EzCatDB: D00003

DB codeD00003
CATH domainDomain 13.40.50.720
Domain 23.30.360.10Catalytic domain
E.C.1.1.1.3
CSA1ebf

CATH domainRelated DB codes (homologues)
3.30.360.10T00219,D00010,D00017,D00023,D00027,D00028,D00034,D00476
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,D00001,D00002,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

Enzyme Name
Swiss-protKEGG

P31116
Protein nameHomoserine dehydrogenasehomoserine dehydrogenase
HSDH
HSD
SynonymsHDH
EC 1.1.1.3

KEGG pathways
MAP codePathways
MAP00260Glycine, serine and threonine metabolism
MAP00300Lysine biosynthesis

Swiss-prot:Accession NumberP31116
Entry nameDHOM_YEAST
ActivityL-homoserine + NAD(P)(+) = L-aspartate 4- semialdehyde + NAD(P)H.
SubunitHomodimer.
Subcellular location
Cofactor


SubstratesProducts
KEGG-idC00263C00003C00006C00441C00004C00005C00080
CompoundL-HomoserineNAD+NADP+L-Aspartate 4-semialdehydeNADHNADPHH+
Typeamino acids,carbohydrateamide group,amine group,nucleotideamide group,amine group,nucleotideamino acids,carbohydrateamide group,amine group,nucleotideamide group,amine group,nucleotideothers
1ebfA01UnboundBound:NADUnboundUnboundUnboundUnbound
1ebfB01UnboundUnboundUnboundUnboundUnboundUnbound
1ebuA01UnboundUnboundUnboundUnboundUnboundUnbound
1ebuB01UnboundUnboundUnboundUnboundUnboundUnbound
1ebuC01UnboundUnboundUnboundUnboundUnboundUnbound
1ebuD01UnboundAnalogue:NDAUnboundUnboundUnboundUnbound
1q7gA01UnboundAnalogue:NHOUnboundUnboundUnboundUnbound
1q7gB01UnboundUnboundUnboundUnboundUnboundUnbound
1tveA01UnboundUnboundUnboundUnboundUnboundUnbound
1tveB01UnboundUnboundUnboundUnboundUnboundUnbound
1ebfA02UnboundUnboundUnboundUnboundUnboundUnbound
1ebfB02UnboundUnboundUnboundUnboundUnboundUnbound
1ebuA02UnboundUnboundUnboundUnboundUnboundUnbound
1ebuB02UnboundUnboundUnboundUnboundUnboundUnbound
1ebuC02UnboundUnboundUnboundUnboundUnboundUnbound
1ebuD02Bound:HSEUnboundUnboundUnboundUnboundUnbound
1q7gA02UnboundUnboundUnboundUnboundUnboundUnbound
1q7gB02UnboundUnboundUnboundUnboundUnboundUnbound
1tveA02UnboundUnboundUnboundUnboundUnboundUnbound
1tveB02UnboundUnboundUnboundUnboundUnboundUnbound

Active-site residues
resource
literature [12]
pdbCatalytic residues
1ebfA01
1ebfB01
1ebuA01
1ebuB01
1ebuC01
1ebuD01
1q7gA01
1q7gB01
1tveA01
1tveB01
1ebfA02ASP 219;LYS 223
1ebfB02ASP 219;LYS 223
1ebuA02ASP 219;LYS 223
1ebuB02ASP 219;LYS 223
1ebuC02ASP 219;LYS 223
1ebuD02ASP 219;LYS 223
1q7gA02ASP 219;LYS 223
1q7gB02ASP 219;LYS 223
1tveA02ASP 219;LYS 223
1tveB02ASP 219;LYS 223

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[12]Fig.5a, p.242-243
[13]Scheme 1, Scheme 2, p.51-53

references
[1]
PubMed ID4388077
JournalBiochim Biophys Acta
Year1969
Volume171
Pages205-16
AuthorsBryan JK
TitleStudies on the catalytic and regulatory properties of homoserine dehydrogenase of Zea mays roots.
[2]
PubMed ID4397398
JournalBiochim Biophys Acta
Year1971
Volume235
Pages1-13
AuthorsBothwell MA, Datta P
TitleEffects of K+ on the catalytic and regulatory properties of homoserine dehydrogenase of Pseudomonas fluorescens.
[3]
PubMed ID4562990
JournalEur J Biochem
Year1972
Volume28
Pages520-7
AuthorsVeron M, Falcoz-Kelly F, Cohen GN
TitleThe threonine-sensitive homoserine dehydrogenase and aspartokinase activities of Escherichia coli K12. The two catalytic activities are carried by two independent regions of the polypeptide chain.
[4]
PubMed ID4149354
JournalEur J Biochem
Year1973
Volume38
Pages325-35
AuthorsVeron M, Saari JC, Villar-Palasi C, Cohen GN
TitleThe threonine-sensitive homoserine dehydrogenase and aspartokinase activities of Escherichia coli K 12. Intra and intersubunit interactions between the catalytic regions of the bifunctional enzyme.
[5]
PubMed ID182215
JournalBiochemistry
Year1976
Volume15
Pages3704-10
AuthorsWright JK, Feldman J, Takahashi M
TitleCobalt(III) affinity-labeled aspartokinase. Formation of substrate and inhibitor adducts.
[6]
PubMed ID414912
JournalEur J Biochem
Year1978
Volume82
Pages453-61
AuthorsEpstein CC, Datta P
TitleHomoserine dehydrogenase of Rhodospirillum rubrum. Physical and chemical characterization.
[7]
PubMed ID6774337
JournalProc Natl Acad Sci U S A
Year1980
Volume77
Pages3379-83
AuthorsGarel JR, Dautry-Varsat A
TitleSequential folding of a bifunctional allosteric protein.
[8]
PubMed ID6365907
JournalJ Biol Chem
Year1984
Volume259
Pages2252-6
AuthorsMuller K, Garel JR
TitleThe interaction between Escherichia coli aspartokinase-homoserine dehydrogenase and 3-acetylpyridine-adenine dinucleotide phosphate (reduced), an analog of NADPH.
[9]
PubMed ID2241177
JournalArch Biochem Biophys
Year1990
Volume283
Pages96-101
AuthorsAngeles TS, Viola RE
TitleThe kinetic mechanisms of the bifunctional enzyme aspartokinase-homoserine dehydrogenase I from Escherichia coli.
[10]
PubMed ID8432719
JournalJ Bacteriol
Year1993
Volume175
Pages959-65
AuthorsOmori K, Komatsubara S
TitleRole of serine 352 in the allosteric response of Serratia marcescens aspartokinase I-homoserine dehydrogenase I analyzed by using site-directed mutagenesis.
[11]
PubMed ID9761913
JournalActa Crystallogr D Biol Crystallogr
Year1998
Volume54
Pages413-5
AuthorsDeLaBarre B, Jacques SL, Pratt CE, Ruth DA, Wright GD, Berghuis AM
TitleCrystallization and preliminary X-ray diffraction studies of homoserine dehydrogenase from Saccharomyces cerevisiae.
[12]
CommentsX-ray crystallography
PubMed ID10700284
JournalNat Struct Biol
Year2000
Volume7
Pages238-44
AuthorsDeLaBarre B, Thompson PR, Wright GD, Berghuis AM
TitleCrystal structures of homoserine dehydrogenase suggest a novel catalytic mechanism for oxidoreductases.
Related PDB1ebf,1ebu
[13]
PubMed ID11341915
JournalBiochim Biophys Acta
Year2001
Volume1544
Pages42-54
AuthorsJacques SL, Ejim LJ, Wright GD
TitleHomoserine dehydrogenase from Saccharomyces cerevisiae: kinetic mechanism and stereochemistry of hydride transfer.
[14]
PubMed ID11341914
JournalBiochim Biophys Acta
Year2001
Volume1544
Pages28-41
AuthorsJacques SL, Nieman C, Bareich D, Broadhead G, Kinach R, Honek JF, Wright GD
TitleCharacterization of yeast homoserine dehydrogenase, an antifungal target: the invariant histidine 309 is important for enzyme integrity.
[15]
PubMed ID11888289
JournalBiochemistry
Year2002
Volume41
Pages3720-5
AuthorsJames CL, Viola RE
TitleProduction and characterization of bifunctional enzymes. Domain swapping to produce new bifunctional enzymes in the aspartate pathway.
[16]
CommentsX-ray crystallography
PubMed ID14583265
JournalChem Biol
Year2003
Volume10
Pages989-95
AuthorsJacques SL, Mirza IA, Ejim L, Koteva K, Hughes DW, Green K, Kinach R, Honek JF, Lai HK, Berghuis AM, Wright GD
TitleEnzyme-assisted suicide: molecular basis for the antifungal activity of 5-hydroxy-4-oxonorvaline by potent inhibition of homoserine dehydrogenase.
Related PDB1q7g
[17]
PubMed ID15210149
JournalBioorg Med Chem
Year2004
Volume12
Pages3825-30
AuthorsEjim L, Mirza IA, Capone C, Nazi I, Jenkins S, Chee GL, Berghuis AM, Wright GD
TitleNew phenolic inhibitors of yeast homoserine dehydrogenase.
Related PDB1tve


createdupdated
2004-03-242009-02-26
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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