EzCatDB: D00001

DB codeD00001
CATH domainDomain 13.90.180.10Catalytic domain
Domain 23.40.50.720Catalytic domain
E.C.1.1.1.1
CSA1qlh
MACiEM0256

CATH domainRelated DB codes (homologues)
3.40.50.720S00543,S00551,S00552,S00553,S00602,S00604,S00605,S00608,S00610,S00625,S00319,S00328,S00329,S00330,S00331,S00332,D00456,D00457,D00458,S00324,S00320,S00325,S00326,S00327,D00459,S00335,S00336,S00334,T00219,S00339,D00513,D00002,D00003,D00005,D00007,D00008,D00010,D00012,D00017,D00018,D00023,D00027,D00028,D00031,D00032,D00033,D00034,D00035,D00037,D00048,D00071,D00476,D00481,D00482,D00490,D00492,D00494,D00545,D00601,D00603,D00604,D00605,D00615,D00845,D00857,D00858,M00161,M00171,M00210,T00002,T00010,T00011,T00015,T00227,T00247,T00408,T00414,D00827,D00262,D00274,D00275,M00035,T00109
3.90.180.10D00002,D00018,D00048,D00481,D00482,D00490,D00492,D00615

Enzyme Name
Swiss-protKEGG

P00326P00327P00328
Protein nameAlcohol dehydrogenase 1CAlcohol dehydrogenase E chainAlcohol dehydrogenase S chainalcohol dehydrogenase
aldehyde reductase
ADH
alcohol dehydrogenase (NAD)
aliphatic alcohol dehydrogenase
ethanol dehydrogenase
NAD-dependent alcohol dehydrogenase
NAD-specific aromatic alcohol dehydrogenase
NADH-alcohol dehydrogenase
NADH-aldehyde dehydrogenase
primary alcohol dehydrogenase
yeast alcohol dehydrogenase
SynonymsEC 1.1.1.1
Alcohol dehydrogenase subunit gamma
EC 1.1.1.1
EC 1.1.1.1

KEGG pathways
MAP codePathways
MAP00010Glycolysis / Gluconeogenesis
MAP00071Fatty acid metabolism
MAP00120Bile acid biosynthesis
MAP00260Glycine, serine and threonine metabolism
MAP00350Tyrosine metabolism
MAP006241- and 2-Methylnaphthalene degradation
MAP006413-Chloroacrylic acid degradation
MAP00830Retinol metabolism
MAP00980Metabolism of xenobiotics by cytochrome P450
MAP00982Drug metabolism - cytochrome P450

Swiss-prot:Accession NumberP00326P00327P00328
Entry nameADH1G_HUMANADH1E_HORSEADH1S_HORSE
ActivityAn alcohol + NAD(+) = an aldehyde or ketone + NADH.An alcohol + NAD(+) = an aldehyde or ketone + NADH.An alcohol + NAD(+) = an aldehyde or ketone + NADH.
SubunitDimer of identical or non-identical chains of three types, alpha, beta and gamma.Dimer of identical or non-identical chains of two types (E and S) coded by 2 separate genes at different loci.Dimer of identical or non-identical chains of two types (E and S) coded by 2 separate genes at different loci.
Subcellular locationCytoplasm.Cytoplasm.Cytoplasm.
CofactorBinds 2 zinc ions per subunit.Binds 2 zinc ions per subunit.Binds 2 zinc ions per subunit (By similarity).


CofactorsSubstratesProducts
KEGG-idC00038C00003C00226C00069C00004C00071C00709C00080
CompoundZincNAD+Primary alcoholAlcoholNADHAldehydeKetoneH+
Typeheavy metalamide group,amine group,nucleotidecarbohydratecarbohydrateamide group,amine group,nucleotidecarbohydratecarbohydrateothers
1ht0A01Bound:2x_ZNUnboundUnboundUnboundUnboundUnboundUnbound
1ht0B01Bound:2x_ZNUnboundUnboundUnboundUnboundUnboundUnbound
1a71A01Bound:2x_ZNUnboundAnalogue:ETFUnboundUnboundUnboundUnbound
1a71B01Bound:2x_ZNUnboundAnalogue:ETFUnboundUnboundUnboundUnbound
1a72A01Bound:2x_ZNUnboundUnboundUnboundUnboundUnboundUnbound
1adbA01Bound:2x_ZNUnboundBound:EOHUnboundUnboundUnboundUnbound
1adbB01Bound:2x_ZNUnboundBound:EOHUnboundUnboundUnboundUnbound
1adcA01Bound:2x_ZNUnboundBound:EOHUnboundUnboundUnboundUnbound
1adcB01Bound:2x_ZNUnboundBound:EOHUnboundUnboundUnboundUnbound
1adfA01Bound:2x_ZNUnboundUnboundUnboundUnboundUnboundUnbound
1adgA01Bound:2x_ZNUnboundUnboundUnboundUnboundUnboundUnbound
1axeA01Bound:2x_ZNUnboundAnalogue:ETFUnboundUnboundUnboundUnbound
1axeB01Bound:2x_ZNUnboundAnalogue:ETFUnboundUnboundUnboundUnbound
1axgA01Bound:2x_ZNUnboundAnalogue:ETFUnboundUnboundUnboundUnbound
1axgB01Bound:2x_ZNUnboundAnalogue:ETFUnboundUnboundUnboundUnbound
1axgC01Bound:2x_ZNUnboundAnalogue:ETFUnboundUnboundUnboundUnbound
1axgD01Bound:2x_ZNUnboundAnalogue:ETFUnboundUnboundUnboundUnbound
1btoA01Bound:2x_ZNUnboundUnboundUnboundUnboundUnboundAnalogue:SSB
1btoB01Bound:2x_ZNUnboundUnboundUnboundUnboundUnboundAnalogue:SSB
1btoC01Bound:2x_ZNUnboundUnboundUnboundUnboundUnboundAnalogue:SSB
1btoD01Bound:2x_ZNUnboundUnboundUnboundUnboundUnboundAnalogue:SSB
1hetA01Bound:2x_ZNUnboundUnboundBound:MRDUnboundUnboundUnbound
1hetB01Bound:2x_ZNUnboundUnboundBound:MRDUnboundUnboundUnbound
1heuA01Analogue:2x_CDUnboundUnboundBound:MRDUnboundUnboundUnbound
1heuB01Analogue:2x_CDUnboundUnboundBound:MRDUnboundUnboundUnbound
1hldA01Bound:2x_ZNUnboundAnalogue:PFB,BRBUnboundUnboundUnboundUnbound
1hldB01Bound:2x_ZNUnboundAnalogue:PFB,BRBUnboundUnboundUnboundUnbound
1ju9A01Bound:2x_ZNUnboundUnboundUnboundUnboundUnboundUnbound
1ju9B01Bound:2x_ZNUnboundUnboundUnboundUnboundUnboundUnbound
1ldeA01Bound:2x_ZNUnboundUnboundUnboundUnboundAnalogue:FPIUnbound
1ldeB01Bound:2x_ZNUnboundUnboundUnboundUnboundAnalogue:FPIUnbound
1ldeC01Bound:2x_ZNUnboundUnboundUnboundUnboundAnalogue:FPIUnbound
1ldeD01Bound:2x_ZNUnboundUnboundUnboundUnboundAnalogue:FPIUnbound
1ldyA01Bound:2x_ZNUnboundUnboundUnboundUnboundAnalogue:CXFUnbound
1ldyB01Bound:2x_ZNUnboundUnboundUnboundUnboundAnalogue:CXFUnbound
1ldyC01Bound:2x_ZNUnboundUnboundUnboundUnboundAnalogue:CXFUnbound
1ldyD01Bound:2x_ZNUnboundUnboundUnboundUnboundAnalogue:CXFUnbound
1mg0A01Bound:2x_ZNUnboundAnalogue:DFBUnboundUnboundUnboundUnbound
1mg0B01Bound:2x_ZNUnboundAnalogue:DFBUnboundUnboundUnboundUnbound
1mg0C01Bound:2x_ZNUnboundAnalogue:DFBUnboundUnboundUnboundUnbound
1mg0D01Bound:2x_ZNUnboundAnalogue:DFBUnboundUnboundUnboundUnbound
1mgoA01Bound:2x_ZNUnboundUnboundUnboundUnboundUnboundUnbound
1mgoB01Bound:2x_ZNUnboundUnboundBound:MPDUnboundUnboundUnbound
1n8kA01Bound:2x_ZNUnboundUnboundUnboundUnboundUnboundUnbound
1n8kB01Bound:2x_ZNUnboundUnboundUnboundUnboundUnboundUnbound
1n92A01Bound:2x_ZNUnboundUnboundUnboundUnboundUnboundUnbound
1n92B01Bound:2x_ZNUnboundUnboundUnboundUnboundUnboundUnbound
1p1rA01Bound:2x_ZNUnboundUnboundUnboundUnboundAnalogue:NMHUnbound
1p1rB01Bound:2x_ZNUnboundUnboundUnboundUnboundAnalogue:NMHUnbound
1p1rC01Bound:2x_ZNUnboundUnboundUnboundUnboundAnalogue:NMHUnbound
1p1rD01Bound:2x_ZNUnboundUnboundUnboundUnboundAnalogue:NMHUnbound
1qlhA01Bound:2x_ZNUnboundUnboundUnboundUnboundUnboundUnbound
1qljA01Bound:2x_ZNUnboundUnboundUnboundUnboundUnboundUnbound
1qv6A01Bound:2x_ZNUnboundAnalogue:24BUnboundUnboundUnboundUnbound
1qv6B01Bound:2x_ZNUnboundAnalogue:24BUnboundUnboundUnboundUnbound
1qv7A01Bound:2x_ZNUnboundAnalogue:DFBUnboundUnboundUnboundUnbound
1qv7B01Bound:2x_ZNUnboundAnalogue:DFBUnboundUnboundUnboundUnbound
2ohxA01Bound:2x_ZNUnboundUnboundUnboundUnboundUnboundAnalogue:DMS
2ohxB01Bound:2x_ZNUnboundUnboundUnboundUnboundUnboundAnalogue:DMS
2oxiA01Bound:_ZN,Analogue;_CUUnboundUnboundUnboundUnboundUnboundAnalogue:DMS
2oxiB01Bound:_ZN,Analogue;_CUUnboundUnboundUnboundUnboundUnboundAnalogue:DMS
3btoA01Bound:2x_ZNUnboundUnboundUnboundUnboundUnboundAnalogue:SSB
3btoB01Bound:2x_ZNUnboundUnboundUnboundUnboundUnboundAnalogue:SSB
3btoC01Bound:2x_ZNUnboundUnboundUnboundUnboundUnboundAnalogue:SSB
3btoD01Bound:2x_ZNUnboundUnboundUnboundUnboundUnboundAnalogue:SSB
5adhA01Bound:2x_ZNUnboundUnboundBound:MPDUnboundUnboundUnbound
6adhA01Bound:2x_ZNUnboundUnboundUnboundUnboundUnboundAnalogue:DMS
6adhB01Bound:2x_ZNUnboundUnboundUnboundUnboundUnboundAnalogue:DMS
7adhA01Bound:2x_ZNUnboundUnboundUnboundUnboundUnboundUnbound
8adhA01Bound:2x_ZNUnboundUnboundUnboundUnboundUnboundUnbound
1ee2A01Bound:2x_ZNUnboundUnboundUnboundUnboundUnboundAnalogue:CHD
1ee2B01Bound:2x_ZNUnboundUnboundUnboundUnboundUnboundAnalogue:CHD
1ht0A02UnboundBound:NADUnboundUnboundUnboundUnboundUnbound
1ht0B02UnboundBound:NADUnboundUnboundUnboundUnboundUnbound
1a71A02UnboundBound:NADUnboundUnboundUnboundUnboundUnbound
1a71B02UnboundBound:NADUnboundUnboundUnboundUnboundUnbound
1a72A02UnboundAnalogue:PADUnboundUnboundUnboundUnboundUnbound
1adbA02UnboundAnalogue:CNDUnboundUnboundUnboundUnboundUnbound
1adbB02UnboundAnalogue:CNDUnboundUnboundUnboundUnboundUnbound
1adcA02UnboundAnalogue:PADUnboundUnboundUnboundUnboundUnbound
1adcB02UnboundAnalogue:PADUnboundUnboundUnboundUnboundUnbound
1adfA02UnboundAnalogue:TADUnboundUnboundUnboundUnboundUnbound
1adgA02UnboundAnalogue:SADUnboundUnboundUnboundUnboundUnbound
1axeA02UnboundBound:NADUnboundUnboundUnboundUnboundUnbound
1axeB02UnboundBound:NADUnboundUnboundUnboundUnboundUnbound
1axgA02UnboundBound:NADUnboundUnboundUnboundUnboundUnbound
1axgB02UnboundBound:NADUnboundUnboundUnboundUnboundUnbound
1axgC02UnboundBound:NADUnboundUnboundUnboundUnboundUnbound
1axgD02UnboundBound:NADUnboundUnboundUnboundUnboundUnbound
1btoA02UnboundUnboundUnboundUnboundBound:NADUnboundUnbound
1btoB02UnboundUnboundUnboundUnboundBound:NADUnboundUnbound
1btoC02UnboundUnboundUnboundUnboundBound:NADUnboundUnbound
1btoD02UnboundUnboundUnboundUnboundBound:NADUnboundUnbound
1hetA02UnboundBound:NADUnboundUnboundBound:NADUnboundUnbound
1hetB02UnboundBound:NADUnboundUnboundBound:NADUnboundUnbound
1heuA02UnboundBound:NADUnboundUnboundBound:NADUnboundUnbound
1heuB02UnboundBound:NADUnboundUnboundBound:NADUnboundUnbound
1hldA02UnboundBound:NADAnalogue:PFB,BRBUnboundUnboundUnboundUnbound
1hldB02UnboundBound:NADAnalogue:PFB,BRBUnboundUnboundUnboundUnbound
1ju9A02UnboundAnalogue:NADUnboundUnboundUnboundUnboundUnbound
1ju9B02UnboundAnalogue:NADUnboundUnboundUnboundUnboundUnbound
1ldeA02UnboundUnboundUnboundUnboundBound:NADUnboundUnbound
1ldeB02UnboundUnboundUnboundUnboundBound:NADUnboundUnbound
1ldeC02UnboundUnboundUnboundUnboundBound:NADUnboundUnbound
1ldeD02UnboundUnboundUnboundUnboundBound:NADUnboundUnbound
1ldyA02UnboundUnboundUnboundUnboundBound:NADUnboundUnbound
1ldyB02UnboundUnboundUnboundUnboundBound:NADUnboundUnbound
1ldyC02UnboundUnboundUnboundUnboundBound:NADUnboundUnbound
1ldyD02UnboundUnboundUnboundUnboundBound:NADUnboundUnbound
1mg0A02UnboundBound:NADUnboundUnboundUnboundUnboundUnbound
1mg0B02UnboundBound:NADUnboundUnboundUnboundUnboundUnbound
1mg0C02UnboundBound:NADUnboundUnboundUnboundUnboundUnbound
1mg0D02UnboundBound:NADUnboundUnboundUnboundUnboundUnbound
1mgoA02UnboundBound:NADUnboundUnboundUnboundUnboundUnbound
1mgoB02UnboundBound:NADUnboundUnboundUnboundUnboundUnbound
1n8kA02UnboundAnalogue:NAJ-PZOUnboundUnboundUnboundUnboundUnbound
1n8kB02UnboundAnalogue:NAJ-PZOUnboundUnboundUnboundUnboundUnbound
1n92A02UnboundAnalogue:NAJ-PYZUnboundUnboundUnboundUnboundUnbound
1n92B02UnboundAnalogue:NAJ-PYZUnboundUnboundUnboundUnboundUnbound
1p1rA02UnboundUnboundUnboundUnboundBound:NAJUnboundUnbound
1p1rB02UnboundUnboundUnboundUnboundBound:NAJUnboundUnbound
1p1rC02UnboundUnboundUnboundUnboundBound:NAJUnboundUnbound
1p1rD02UnboundUnboundUnboundUnboundBound:NAJUnboundUnbound
1qlhA02UnboundBound:NADUnboundUnboundUnboundUnboundUnbound
1qljA02UnboundUnboundUnboundUnboundUnboundUnboundUnbound
1qv6A02UnboundBound:NADUnboundUnboundUnboundUnboundUnbound
1qv6B02UnboundBound:NADUnboundUnboundUnboundUnboundUnbound
1qv7A02UnboundBound:NADUnboundUnboundUnboundUnboundUnbound
1qv7B02UnboundBound:NADUnboundUnboundUnboundUnboundUnbound
2ohxA02UnboundUnboundUnboundUnboundBound:NADUnboundUnbound
2ohxB02UnboundUnboundUnboundUnboundBound:NADUnboundUnbound
2oxiA02UnboundUnboundUnboundUnboundBound:NADUnboundUnbound
2oxiB02UnboundUnboundUnboundUnboundBound:NADUnboundUnbound
3btoA02UnboundUnboundUnboundUnboundBound:NADUnboundUnbound
3btoB02UnboundUnboundUnboundUnboundBound:NADUnboundUnbound
3btoC02UnboundUnboundUnboundUnboundBound:NADUnboundUnbound
3btoD02UnboundUnboundUnboundUnboundBound:NADUnboundUnbound
5adhA02UnboundAnalogue:APRUnboundUnboundUnboundUnboundUnbound
6adhA02UnboundBound:NADUnboundUnboundUnboundUnboundUnbound
6adhB02UnboundBound:NADUnboundUnboundUnboundUnboundUnbound
7adhA02UnboundUnboundUnboundUnboundUnboundUnboundUnbound
8adhA02UnboundUnboundUnboundUnboundUnboundUnboundUnbound
1ee2A02UnboundBound:NADUnboundUnboundUnboundUnboundUnbound
1ee2B02UnboundBound:NADUnboundUnboundUnboundUnboundUnbound

Active-site residues
resource
Swiss-prot;P00327, P00326, P00328,P26325
pdbCatalytic residuesCofactor-binding residuescomment
1ht0A01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
mutant I349V
1ht0B01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
mutant I349V
1a71A01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
mutant F93W
1a71B01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
mutant F93W
1a72A01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
mutant F93W
1adbA01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)

1adbB01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)

1adcA01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)

1adcB01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)

1adfA01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)

1adgA01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)

1axeA01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
mutant F93W
1axeB01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
mutant F93W
1axgA01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)

1axgB01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)

1axgC01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)

1axgD01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)

1btoA01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)

1btoB01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)

1btoC01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)

1btoD01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)

1hetA01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)

1hetB01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)

1heuA01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)

1heuB01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)

1hldA01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)

1hldB01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)

1ju9A01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)

1ju9B01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)

1ldeA01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)

1ldeB01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)

1ldeC01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)

1ldeD01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)

1ldyA01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)

1ldyB01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)

1ldyC01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)

1ldyD01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)

1mg0A01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
mutant F93A
1mg0B01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
mutant F93A
1mg0C01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
mutant F93A
1mg0D01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
mutant F93A
1mgoA01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
mutant F93A
1mgoB01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
mutant F93A
1n8kA01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)

1n8kB01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)

1n92A01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)

1n92B01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)

1p1rA01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)

1p1rB01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)

1p1rC01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)

1p1rD01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)

1qlhA01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)

1qljA01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)

1qv6A01SER 48;      
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
mutant H51Q
1qv6B01SER 48;      
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
mutant H51Q
1qv7A01SER 48;      
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
mutant H51Q
1qv7B01SER 48;      
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
mutant H51Q
2ohxA01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)

2ohxB01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)

2oxiA01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)

2oxiB01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)

3btoA01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)

3btoB01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)

3btoC01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)

3btoD01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)

5adhA01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)

6adhA01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)

6adhB01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)

7adhA01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)

8adhA01SER 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)

1ee2A01SER 48;HIS 51
CYS 46;HIS 67;CYS 173(Catalytic zinc binding)

1ee2B01SER 48;HIS 51
CYS 46;HIS 67;CYS 173(Catalytic zinc binding)

1ht0A02

mutant R271Q
1ht0B02

mutant R271Q
1a71A02

mutant V203A
1a71B02

mutant V203A
1a72A02

mutant V203A
1adbA02


1adbB02


1adcA02


1adcB02


1adfA02


1adgA02


1axeA02


1axeB02


1axgA02

mutant V203A
1axgB02

mutant V203A
1axgC02

mutant V203A
1axgD02

mutant V203A
1btoA02


1btoB02


1btoC02


1btoD02


1hetA02


1hetB02


1heuA02


1heuB02


1hldA02


1hldB02


1ju9A02

mutant V292S
1ju9B02

mutant V292S
1ldeA02


1ldeB02


1ldeC02


1ldeD02


1ldyA02


1ldyB02


1ldyC02


1ldyD02


1mg0A02


1mg0B02


1mg0C02


1mg0D02


1mgoA02


1mgoB02


1n8kA02

mutant V292T
1n8kB02

mutant V292T
1n92A02


1n92B02


1p1rA02


1p1rB02


1p1rC02


1p1rD02


1qlhA02

mutant G293A, P295T
1qljA02

mutant G293A, P295T
1qv6A02

mutant K228R
1qv6B02

mutant K228R
1qv7A02

mutant K228R
1qv7B02

mutant K228R
2ohxA02


2ohxB02


2oxiA02


2oxiB02


3btoA02


3btoB02


3btoC02


3btoD02


5adhA02


6adhA02


6adhB02


7adhA02


8adhA02


1ee2A02


1ee2B02



References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[4]Scheme 1, p.14356-14357
[10]Fig.4, p.1065-1067
[13]Fig.2, p.619-621, p.624-625
[31]Fig.10, p.5235-5237
[32]p.273
[41]Fig.2, p.9786-9789, p.9790-9791
[42]p.135-136
[53]Scheme 1, p.13957-13959
[57]Chart 1, Chart 2, p.11955-11956, p.11957-11959
[58]Fig.5, p.9320
[60]Scheme 2, p.480
[67]Scheme 1, p.3023-3025
[70]Fig.7, p.3930

references
[1]
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Related Swiss-protP00327,P00328
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PubMed ID202459
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Year1977
Volume81
Pages403-9
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[3]
CommentsX-ray crystallography
PubMed ID7024556
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Volume146
Pages561-87
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Related PDB6adh
[4]
PubMed ID6754727
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Year1982
Volume257
Pages14349-58
AuthorsEklund H, Plapp BV, Samama JP, Branden CI
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Year1984
Volume23
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Related Swiss-protP00327,P00328
[6]
CommentsX-ray crystallography
PubMed ID3771574
JournalJ Biol Chem
Year1986
Volume261
Pages15273-80
AuthorsColonna-Cesari F, Perahia D, Karplus M, Eklund H, Braden CI, Tapia O
TitleInterdomain motion in liver alcohol dehydrogenase. Structural and energetic analysis of the hinge bending mode.
Related PDB5adh,7adh,8adh
[7]
PubMed ID3608931
JournalEur Biophys J
Year1987
Volume14
Pages431-9
AuthorsBertini I, Lanini G, Luchinat C, Haas C, Maret W, Zeppezauer M
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[8]
PubMed ID2322541
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Year1990
Volume29
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PubMed ID1772423
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Year1991
Volume24
Pages451-60
AuthorsFong WP, Keung WM
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[10]
PubMed ID1989677
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Year1991
Volume30
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AuthorsEhrig T, Hurley TD, Edenberg HJ, Bosron WF
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[11]
PubMed ID2054345
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Year1991
Volume30
Pages6397-401
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TitleAn aspartate residue in yeast alcohol dehydrogenase I determines the specificity for coenzyme.
[12]
PubMed ID1807973
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Volume20
Pages215-21
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[13]
PubMed ID1935957
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Year1991
Volume201
Pages615-25
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TitleSubstrate specificity and stereoselectivity of horse liver alcohol dehydrogenase. Kinetic evaluation of binding and activation parameters controlling the catalytic cycles of unbranched, acyclic secondary alcohols and ketones as substrates of the native and active-site-specific Co(II)-substituted enzyme.
[14]
PubMed ID1712777
JournalJ Biol Chem
Year1991
Volume266
Pages13296-302
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[15]
PubMed ID1368113
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Year1992
Volume14
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[16]
PubMed ID1572355
JournalEur J Biochem
Year1992
Volume205
Pages519-26
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TitleA single-residue exchange gives human recombinant beta beta alcohol dehydrogenase gamma gamma isozyme properties.
[17]
PubMed ID1324852
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Year1992
Volume309
Pages92-6
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TitleCopper(II)-substituted horse liver alcohol dehydrogenase: structure of the minor species.
[18]
PubMed ID1544927
JournalJ Biol Chem
Year1992
Volume267
Pages5527-33
AuthorsPark DH, Plapp BV
TitleInterconversion of E and S isoenzymes of horse liver alcohol dehydrogenase. Several residues contribute indirectly to catalysis.
[19]
PubMed ID8493927
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Year1993
Volume328
Pages481-91
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[20]
PubMed ID8493923
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Year1993
Volume328
Pages451-5
AuthorsHubatsch I, Zeppezauer M, Waidelich D, Bayer E
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[21]
PubMed ID8493917
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Year1993
Volume328
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TitleSubstrate specificity of alcohol dehydrogenases.
[22]
PubMed ID8504071
JournalBiochemistry
Year1993
Volume32
Pages5503-7
AuthorsBahnson BJ, Park DH, Kim K, Plapp BV, Klinman JP
TitleUnmasking of hydrogen tunneling in the horse liver alcohol dehydrogenase reaction by site-directed mutagenesis.
[23]
PubMed ID8422379
JournalBiochemistry
Year1993
Volume32
Pages735-8
AuthorsHenehan GT, Oppenheimer NJ
TitleHorse liver alcohol dehydrogenase-catalyzed oxidation of aldehydes: dismutation precedes net production of reduced nicotinamide adenine dinucleotide.
[24]
PubMed ID8218182
JournalBiochemistry
Year1993
Volume32
Pages11186-94
AuthorsShearer GL, Kim K, Lee KM, Wang CK, Plapp BV
TitleAlternative pathways and reactions of benzyl alcohol and benzaldehyde with horse liver alcohol dehydrogenase.
[25]
PubMed ID8490046
JournalBiochim Biophys Acta
Year1993
Volume1163
Pages144-8
AuthorsAdlercreutz P
TitleActivation of enzymes in organic media at low water activity by polyols and saccharides.
[26]
PubMed ID7684231
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Year1993
Volume15
Pages383-92
AuthorsCreagh AL, Prausnitz JM, Blanch HW
TitleStructural and catalytic properties of enzymes in reverse micelles.
[27]
PubMed ID8354263
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Year1993
Volume215
Pages567-72
AuthorsShilton BH, Campbell RL, Walton DJ
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[28]
CommentsX-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS)
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Year1994
Volume50
Pages793-807
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TitleRefined crystal structure of liver alcohol dehydrogenase-NADH complex at 1.8-A resolution.
Related Swiss-protP00327
[29]
CommentsX-ray crystallography
PubMed ID8286346
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Year1994
Volume33
Pages23-32
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TitleCrystallographic studies of two alcohol dehydrogenase-bound analogues of thiazole-4-carboxamide adenine dinucleotide (TAD), the active anabolite of the antitumor agent tiazofurin.
Related PDB1adf,1adg
[30]
CommentsX-ray crystallography
PubMed ID7918390
JournalBiochemistry
Year1994
Volume33
Pages11734-44
AuthorsLi H, Hallows WH, Punzi JS, Pankiewicz KW, Watanabe KA, Goldstein BM
TitleCrystallographic studies of isosteric NAD analogues bound to alcohol dehydrogenase: specificity and substrate binding in two ternary complexes.
Related PDB1adb,1adc
[31]
CommentsX-ray crystallography
PubMed ID8172897
JournalBiochemistry
Year1994
Volume33
Pages5230-7
AuthorsRamaswamy S, Eklund H, Plapp BV
TitleStructures of horse liver alcohol dehydrogenase complexed with NAD+ and substituted benzyl alcohols.
Related PDB1hld
[32]
PubMed ID8032158
JournalEXS
Year1994
Volume71
Pages269-77
AuthorsEklund H, Ramaswamy S, Plapp BV, el-Ahmad M, Danielsson O, Hoog JO, Jornvall H
TitleCrystallographic investigations of alcohol dehydrogenases.
[33]
PubMed ID8127901
JournalProc Natl Acad Sci U S A
Year1994
Volume91
Pages1893-7
AuthorsPares X, Cederlund E, Moreno A, Hjelmqvist L, Farres J, Jornvall H
TitleMammalian class IV alcohol dehydrogenase (stomach alcohol dehydrogenase): structure, origin, and correlation with enzymology.
[34]
PubMed ID7484400
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Year1995
Volume372
Pages365-71
Authorsel-Ahmad M, Ramaswamy S, Danielsson O, Karlsson C, Estonius M, Hoog JO, Eklund H, Jornvall H
TitleCrystallizations of novel forms of alcohol dehydrogenase.
[35]
PubMed ID7484389
JournalAdv Exp Med Biol
Year1995
Volume372
Pages281-94
AuthorsJornvall H, Danielsson O, Hjelmqvist L, Persson B, Shafqat J
TitleThe alcohol dehydrogenase system.
[36]
PubMed ID7766625
JournalBiochemistry
Year1995
Volume34
Pages7145-53
AuthorsHemmingsen L, Bauer R, Bjerrum MJ, Zeppezauer M, Adolph HW, Formicka G, Cedergren-Zeppezauer E
TitleCd-substituted horse liver alcohol dehydrogenase: catalytic site metal coordination geometry and protein conformation.
[37]
PubMed ID7479907
JournalProc Natl Acad Sci U S A
Year1995
Volume92
Pages10904-8
AuthorsHjelmqvist L, Estonius M, Jornvall H
TitleThe vertebrate alcohol dehydrogenase system: variable class II type form elucidates separate stages of enzymogenesis.
[38]
PubMed ID7549877
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Year1995
Volume4
Pages1124-32
AuthorsRyde U
TitleOn the role of Glu-68 in alcohol dehydrogenase.
[39]
PubMed ID8638928
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Year1996
Volume328
Pages173-83
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TitleStructural and sequence comparisons of quinone oxidoreductase, zeta-crystallin, and glucose and alcohol dehydrogenases.
[40]
PubMed ID8713071
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Year1996
Volume317
Pages447-56
AuthorsFarrar JA, Formicka G, Zeppezauer M, Thomson AJ
TitleMagnetic and optical properties of copper-substituted alcohol dehydrogenase: a bisthiolate copper (II) complex.
[41]
PubMed ID8703951
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Year1996
Volume35
Pages9782-91
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TitleMechanism of aldehyde oxidation catalyzed by horse liver alcohol dehydrogenase.
[42]
PubMed ID8695638
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Year1996
Volume1295
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TitleKinetic and modelling studies of NAD+ and poly(ethylene glycol)-bound NAD+ in horse liver alcohol dehydrogenase.
[43]
PubMed ID8917454
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Year1996
Volume241
Pages546-51
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[44]
PubMed ID8612630
JournalEur J Biochem
Year1996
Volume236
Pages563-70
AuthorsHjelmqvist L, Shafqat J, Siddiqi AR, Jornvall H
TitleLinking of isozyme and class variability patterns in the emergence of novel alcohol dehydrogenase functions. Characterization of isozymes in Uromastix hardwickii.
[45]
PubMed ID8898073
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Year1996
Volume395
Pages99-102
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[46]
PubMed ID9220961
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Year1997
Volume36
Pages8743-54
AuthorsAdolph HW, Kiefer M, Cedergren-Zeppezauer E
TitleElectrostatic effects in the kinetics of coenzyme binding to isozymes of alcohol dehydrogenase from horse liver.
[47]
CommentsX-ray crystallography
PubMed ID9003191
JournalBiochemistry
Year1997
Volume36
Pages382-9
AuthorsCho H, Ramaswamy S, Plapp BV
TitleFlexibility of liver alcohol dehydrogenase in stereoselective binding of 3-butylthiolane 1-oxides.
Related PDB1bto,3bto
[48]
CommentsX-ray crystallography
PubMed ID9132002
JournalBiochemistry
Year1997
Volume36
Pages3522-7
AuthorsRamaswamy S, Scholze M, Plapp BV
TitleBinding of formamides to liver alcohol dehydrogenase.
Related PDB1lde,1ldy
[49]
CommentsX-ray crystallography
PubMed ID9371755
JournalProc Natl Acad Sci U S A
Year1997
Volume94
Pages12797-802
AuthorsBahnson BJ, Colby TD, Chin JK, Goldstein BM, Klinman JP
TitleA link between protein structure and enzyme catalyzed hydrogen tunneling.
Related PDB1axe,1axg
[50]
PubMed ID9521768
JournalBiochemistry
Year1998
Volume37
Pages4482-9
AuthorsCho H, Plapp BV
TitleSpecificity of alcohol dehydrogenases for sulfoxides.
[51]
CommentsX-ray crystallography
PubMed ID9649310
JournalBiochemistry
Year1998
Volume37
Pages9295-304
AuthorsColby TD, Bahnson BJ, Chin JK, Klinman JP, Goldstein BM
TitleActive site modifications in a double mutant of liver alcohol dehydrogenase: structural studies of two enzyme-ligand complexes.
Related PDB1a71,1a72
[52]
PubMed ID9485460
JournalBiochemistry
Year1998
Volume37
Pages3068-77
AuthorsPiersma SR, Visser AJ, de Vries S, Duine JA
TitleOptical spectroscopy of nicotinoprotein alcohol dehydrogenase from Amycolatopsis methanolica: a comparison with horse liver alcohol dehydrogenase and UDP-galactose epimerase.
[53]
CommentsX-ray crystallography
PubMed ID10529241
JournalBiochemistry
Year1999
Volume38
Pages13951-9
AuthorsRamaswamy S, Park DH, Plapp BV
TitleSubstitutions in a flexible loop of horse liver alcohol dehydrogenase hinder the conformational change and unmask hydrogen transfer.
Related PDB1qlh,1qlj
[54]
CommentsX-ray crystallography
PubMed ID11041853
JournalBiochemistry
Year2000
Volume39
Pages12885-97
AuthorsAdolph HW, Zwart P, Meijers R, Hubatsch I, Kiefer M, Lamzin V, Cedergren-Zeppezauer E
TitleStructural basis for substrate specificity differences of horse liver alcohol dehydrogenase isozymes.
Related PDB1ee2
[55]
CommentsTheoretical model
PubMed ID10733557
JournalHepatology
Year2000
Volume31
Pages990-6
AuthorsMarschall HU, Oppermann UC, Svensson S, Nordling E, Persson B, Hoog JO, Jornvall H
TitleHuman liver class I alcohol dehydrogenase gammagamma isozyme: the sole cytosolic 3beta-hydroxysteroid dehydrogenase of iso bile acids.
Related PDB1dda
[56]
CommentsX-ray crystallography
PubMed ID11601993
JournalBiochemistry
Year2001
Volume40
Pages12686-94
AuthorsRubach JK, Ramaswamy S, Plapp BV
TitleContributions of valine-292 in the nicotinamide binding site of liver alcohol dehydrogenase and dynamics to catalysis.
Related PDB1ju9
[57]
PubMed ID11724603
JournalJ Am Chem Soc
Year2001
Volume123
Pages11952-9
AuthorsLuo J, Bruice TC
TitleDynamic structures of horse liver alcohol dehydrogenase (HLADH): results of molecular dynamics simulations of HLADH-NAD(+)-PhCH(2)OH, HLADH-NAD(+)-PhCH(2)O(-), and HLADH-NADH-PhCHO.
[58]
CommentsX-ray crystallography
PubMed ID11134046
JournalJ Biol Chem
Year2001
Volume276
Pages9316-21
AuthorsMeijers R, Morris RJ, Adolph HW, Merli A, Lamzin VS, Cedergren-Zeppezauer ES
TitleOn the enzymatic activation of NADH.
Related PDB1het,1heu
[59]
CommentsX-ray crystallography
PubMed ID11274460
JournalProtein Sci
Year2001
Volume10
Pages697-706
AuthorsNiederhut MS, Gibbons BJ, Perez-Miller S, Hurley TD
TitleThree-dimensional structures of the three human class I alcohol dehydrogenases.
Related PDB1hso,1hsz,1ht0
[60]
PubMed ID12491384
JournalAngew Chem Int Ed Engl
Year2002
Volume41
Pages478-81
AuthorsLo HC, Fish RH
TitleBiomimetic NAD(+) models for tandem cofactor regeneration, horse liver alcohol dehydrogenase recognition of 1,4-NADH derivatives, and chiral synthesis.
[61]
CommentsX-ray crystallography
PubMed ID12501206
JournalBiochemistry
Year2002
Volume41
Pages15770-9
AuthorsRubach JK, Plapp BV
TitleMobility of fluorobenzyl alcohols bound to liver alcohol dehydrogenases as determined by NMR and X-ray crystallographic studies.
Related PDB1mg0,1mgo
[62]
PubMed ID11916410
JournalJ Am Chem Soc
Year2002
Volume124
Pages3270-6
AuthorsCaratzoulas S, Mincer JS, Schwartz SD
TitleIdentification of a protein-promoting vibration in the reaction catalyzed by horse liver alcohol dehydrogenase.
[63]
PubMed ID11942822
JournalJ Am Chem Soc
Year2002
Volume124
Pages3858-64
AuthorsKohen A, Jensen JH
TitleBoundary conditions for the Swain-Schaad relationship as a criterion for hydrogen tunneling.
[64]
PubMed ID12481026
JournalProc Natl Acad Sci U S A
Year2002
Volume99
Pages16597-600
AuthorsLuo J, Bruice TC
TitleTen-nanosecond molecular dynamics simulation of the motions of the horse liver alcohol dehydrogenase.PhCH2O- complex.
[65]
CommentsX-ray crystallography
PubMed ID12627956
JournalBiochemistry
Year2003
Volume42
Pages2907-15
AuthorsRubach JK, Plapp BV
TitleAmino acid residues in the nicotinamide binding site contribute to catalysis by horse liver alcohol dehydrogenase.
Related PDB1n8k,1n92
[66]
CommentsX-ray crystallography
PubMed ID12855684
JournalJ Biol Chem
Year2003
Volume278
Pages36699-706
AuthorsVenkataramaiah TH, Plapp BV
TitleFormamides mimic aldehydes and inhibit liver alcohol dehydrogenases and ethanol metabolism.
Related PDB1p1r
[67]
CommentsX-ray crystallography
PubMed ID15023053
JournalBiochemistry
Year2004
Volume43
Pages3014-26
AuthorsLeBrun LA, Park DH, Ramaswamy S, Plapp BV
TitleParticipation of histidine-51 in catalysis by horse liver alcohol dehydrogenase.
Related PDB1qv6,1qv7
[68]
PubMed ID15331786
JournalProc Natl Acad Sci U S A
Year2004
Volume101
Pages13152-6
AuthorsLuo J, Bruice TC
TitleAnticorrelated motions as a driving force in enzyme catalysis: the dehydrogenase reaction.
[69]
PubMed ID15449945
JournalBiochemistry
Year2004
Volume43
Pages12555-62
AuthorsGibbons BJ, Hurley TD
TitleStructure of three class I human alcohol dehydrogenases complexed with isoenzyme specific formamide inhibitors.
Related PDB1u3t
[70]
PubMed ID19011748
JournalCell Mol Life Sci
Year2008
Volume65
Pages3918-35
AuthorsLadenstein R, Winberg JO, Benach J
TitleMedium- and short-chain dehydrogenase/reductase gene and protein families : Structure-function relationships in short-chain alcohol dehydrogenases.

comments
This enzyme belongs to the class I of the zinc-containing alcohol dehydrogenase superfamily.
Although this enzyme binds two zinc ions, only one zinc is involved in catalysis.
According to the literature [4], [10] and [70], the hydride transfer reaction proceeds as follows:
(0) Catalytic zinc ion, which is bound to Cys46, His67 and Cys174 and the hydroxyl group of the substrate alcohol, may lower the pKa of the hydroxyl oxygen of the alcohol, facilitating its deprotonation.
(1) His51 may act as a general base to deprotonate the hydroxyl oxygen, through 2'-hydroxyl group of NAD+ ribose and Ser48 by a proton relay system, leading to an alkoxide transition-state.
(2) The pro-R hydrogen is transferred from the carbon atom of alcohol to the nicotinamide group in the NAD+. Thus, hydride transfer occurs.

createdupdated
2005-01-112010-09-08


Copyright: Nozomi Nagano, JST & CBRC-AIST
Funded by PRESTO/Japan Science and Technology Corporation (JST) (December 2001 - November 2004)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2010)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)

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