EzCatDB: D00458

DB codeD00458
CATH domainDomain 13.40.192.10Catalytic domain
Domain 23.40.50.720
E.C.1.1.1.38
CSA1do8
MACiEM0021

CATH domainRelated DB codes (homologues)
3.40.192.10D00032,D00033,D00035,D00605,D00845,D00857,D00858,M00210,T00010,T00011,T00414
3.40.50.720S00543,S00551,S00552,S00553,S00602,S00604,S00605,S00608,S00610,S00625,S00319,S00328,S00329,S00330,S00331,S00332,D00456,D00457,S00324,S00320,S00325,S00326,S00327,D00459,S00335,S00336,S00334,T00219,S00339,D00513,D00001,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

Enzyme Name
Swiss-protKEGG

P27443P23368
Protein nameNAD-dependent malic enzyme, mitochondrialNAD-dependent malic enzyme, mitochondrialmalate dehydrogenase (oxaloacetate-decarboxylating)
'malic' enzyme
pyruvic-malic carboxylase
NAD+-specific malic enzyme
NAD+-malic enzyme
NAD+-linked malic enzyme
SynonymsNAD-ME
EC 1.1.1.38
NAD-ME
EC 1.1.1.38
Malic enzyme 2

KEGG pathways
MAP codePathways
MAP00620Pyruvate metabolism

Swiss-prot:Accession NumberP27443P23368
Entry nameMAOM_ASCSUMAOM_HUMAN
Activity(S)-malate + NAD(+) = pyruvate + CO(2) + NADH.(S)-malate + NAD(+) = pyruvate + CO(2) + NADH.
SubunitHomotetramer (By similarity).Homotetramer.
Subcellular locationMitochondrion matrix.Mitochondrion matrix.
CofactorDivalent metal cations. Prefers magnesium or manganese.Divalent metal cations. Prefers magnesium or manganese.


CofactorsSubstratesProductsintermediates
KEGG-idC02148C00149C00003C00006C00022C00011C00004C00005C00036I00001
CompoundDivalent metal(S)-MalateNAD+NADPPyruvateCO2NADHNADPHOxaloacetateEnolpyruvate
Typedivalent metal (Ca2+, Mg2+)carbohydrate,carboxyl groupamide group,amine group,nucleotideamide group,amine group,nucleotidecarbohydrate,carboxyl groupothersamide group,amine group,nucleotideamide group,amine group,nucleotide

1llqA01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1llqB01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1o0sA01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1o0sB01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1do8A01Bound:_MNUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundIntermediate-analogue:OXL
1do8B01Bound:_MNUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundIntermediate-analogue:OXL
1do8C01Bound:_MNUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundIntermediate-analogue:OXL
1do8D01Bound:_MNUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundIntermediate-analogue:OXL
1efkA01Bound:_MGUnboundUnboundUnboundUnboundUnboundUnboundUnboundIntermediate-analogue:MAKUnbound
1efkB01Bound:_MGUnboundUnboundUnboundUnboundUnboundUnboundUnboundIntermediate-analogue:MAKUnbound
1efkC01Bound:_MGUnboundUnboundUnboundUnboundUnboundUnboundUnboundIntermediate-analogue:MAKUnbound
1efkD01Bound:_MGUnboundUnboundUnboundUnboundUnboundUnboundUnboundIntermediate-analogue:MAKUnbound
1eflA01Bound:_MGAnalogue:TTNUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1eflB01Bound:_MGAnalogue:TTNUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1eflC01Bound:_MGAnalogue:TTNUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1eflD01Bound:_MGAnalogue:TTNUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1gz3A01Bound:_MNUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundIntermediate-analogue:OXL
1gz3B01Bound:_MNUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundIntermediate-analogue:OXL
1gz3C01Bound:_MNUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundIntermediate-analogue:OXL
1gz3D01Bound:_MNUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundIntermediate-analogue:OXL
1gz4A01Bound:_MNAnalogue:TTNUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1gz4B01Bound:_MNAnalogue:TTNUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1gz4C01Bound:_MNAnalogue:TTNUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1gz4D01Bound:_MNAnalogue:TTNUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1pj2A01Bound:_MNBound:MLTUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1pj2B01Bound:_MNBound:MLTUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1pj2C01Bound:_MNBound:MLTUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1pj2D01Bound:_MNBound:MLTUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1pj3A01Bound:_MNUnboundUnboundUnboundBound:PYRUnboundUnboundUnboundUnboundUnbound
1pj3B01Bound:_MNUnboundUnboundUnboundBound:PYRUnboundUnboundUnboundUnboundUnbound
1pj3C01Bound:_MNUnboundUnboundUnboundBound:PYRUnboundUnboundUnboundUnboundUnbound
1pj3D01Bound:_MNUnboundUnboundUnboundBound:PYRUnboundUnboundUnboundUnboundUnbound
1pj4A01Bound:_MNBound:MLTUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1pj4B01Bound:_MNBound:MLTUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1pj4C01Bound:_MNBound:MLTUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1pj4D01Bound:_MNBound:MLTUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1pjlA01Analogue:_LUUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1pjlB01Analogue:_LUUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1pjlC01Analogue:_LUUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1pjlD01Analogue:_LUUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1pjlE01Analogue:_LUUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1pjlF01Analogue:_LUUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1pjlG01Analogue:_LUUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1pjlH01Analogue:_LUUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1qr6A01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1qr6B01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1llqA02UnboundUnboundBound:NADUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1llqB02UnboundUnboundBound:NADUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1o0sA02UnboundUnboundUnboundUnboundUnboundUnboundBound:NAIUnboundUnboundUnbound
1o0sB02UnboundUnboundUnboundUnboundUnboundUnboundBound:NAIUnboundUnboundUnbound
1do8A02UnboundUnboundBound:NAD 601UnboundUnboundUnboundUnboundUnboundUnboundUnbound
1do8B02UnboundUnboundBound:NAD 1601UnboundUnboundUnboundUnboundUnboundUnboundUnbound
1do8C02UnboundUnboundBound:NAD 2601UnboundUnboundUnboundUnboundUnboundUnboundUnbound
1do8D02UnboundUnboundBound:NAD 3601UnboundUnboundUnboundUnboundUnboundUnboundUnbound
1efkA02UnboundUnboundBound:NAD 601UnboundUnboundUnboundUnboundUnboundUnboundUnbound
1efkB02UnboundUnboundBound:NAD 1601UnboundUnboundUnboundUnboundUnboundUnboundUnbound
1efkC02UnboundUnboundBound:NAD 2601UnboundUnboundUnboundUnboundUnboundUnboundUnbound
1efkD02UnboundUnboundBound:NAD 3601UnboundUnboundUnboundUnboundUnboundUnboundUnbound
1eflA02UnboundUnboundBound:NAD 601UnboundUnboundUnboundUnboundUnboundUnboundUnbound
1eflB02UnboundUnboundBound:NAD 1601UnboundUnboundUnboundUnboundUnboundUnboundUnbound
1eflC02UnboundUnboundBound:NAD 2601UnboundUnboundUnboundUnboundUnboundUnboundUnbound
1eflD02UnboundUnboundBound:NAD 3601UnboundUnboundUnboundUnboundUnboundUnboundUnbound
1gz3A02UnboundUnboundAnalogue:ATPUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1gz3B02UnboundUnboundAnalogue:ATPUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1gz3C02UnboundUnboundAnalogue:ATPUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1gz3D02UnboundUnboundAnalogue:ATPUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1gz4A02UnboundUnboundAnalogue:ATPUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1gz4B02UnboundUnboundAnalogue:ATPUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1gz4C02UnboundUnboundAnalogue:ATPUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1gz4D02UnboundUnboundAnalogue:ATPUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1pj2A02UnboundUnboundUnboundUnboundUnboundUnboundBound:NAIUnboundUnboundUnbound
1pj2B02UnboundUnboundUnboundUnboundUnboundUnboundBound:NAIUnboundUnboundUnbound
1pj2C02UnboundUnboundUnboundUnboundUnboundUnboundBound:NAIUnboundUnboundUnbound
1pj2D02UnboundUnboundUnboundUnboundUnboundUnboundBound:NAIUnboundUnboundUnbound
1pj3A02UnboundUnboundBound:NAD 601UnboundUnboundUnboundUnboundUnboundUnboundUnbound
1pj3B02UnboundUnboundBound:NAD 1601UnboundUnboundUnboundUnboundUnboundUnboundUnbound
1pj3C02UnboundUnboundBound:NAD 2601UnboundUnboundUnboundUnboundUnboundUnboundUnbound
1pj3D02UnboundUnboundBound:NAD 3601UnboundUnboundUnboundUnboundUnboundUnboundUnbound
1pj4A02UnboundUnboundAnalogue:ATPUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1pj4B02UnboundUnboundAnalogue:ATPUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1pj4C02UnboundUnboundAnalogue:ATPUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1pj4D02UnboundUnboundAnalogue:ATPUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1pjlA02UnboundUnboundBound:NAD 601UnboundUnboundUnboundUnboundUnboundUnboundUnbound
1pjlB02UnboundUnboundBound:NAD 1601UnboundUnboundUnboundUnboundUnboundUnboundUnbound
1pjlC02UnboundUnboundBound:NAD 2601UnboundUnboundUnboundUnboundUnboundUnboundUnbound
1pjlD02UnboundUnboundBound:NAD 3601UnboundUnboundUnboundUnboundUnboundUnboundUnbound
1pjlE02UnboundUnboundBound:NAD 4601UnboundUnboundUnboundUnboundUnboundUnboundUnbound
1pjlF02UnboundUnboundBound:NAD 5601UnboundUnboundUnboundUnboundUnboundUnboundUnbound
1pjlG02UnboundUnboundBound:NAD 6601UnboundUnboundUnboundUnboundUnboundUnboundUnbound
1pjlH02UnboundUnboundBound:NAD 7601UnboundUnboundUnboundUnboundUnboundUnboundUnbound
1qr6A02UnboundUnboundBound:NAD 601UnboundUnboundUnboundUnboundUnboundUnboundUnbound
1qr6B02UnboundUnboundBound:NAD 1601UnboundUnboundUnboundUnboundUnboundUnboundUnbound

Active-site residues
resource
literature [13]
pdbCatalytic residuesCofactor-binding residuescomment
1llqA01TYR  126;LYS  199;ASP  295
GLU  271;ASP  272;ASP  295(Divalent metal binding)

1llqB01TYR  126;LYS  199;ASP  295
GLU  271;ASP  272;ASP  295(Divalent metal binding)

1o0sA01TYR  126;LYS  199;ASP  295
GLU  271;ASP  272;ASP  295(Divalent metal binding)

1o0sB01TYR  126;LYS  199;ASP  295
GLU  271;ASP  272;ASP  295(Divalent metal binding)

1do8A01TYR  112;LYS  183;ASP  279
GLU  255;ASP  256;ASP  279(Divalent metal binding)

1do8B01TYR  112;LYS  183;ASP  279
GLU  255;ASP  256;ASP  279(Divalent metal binding)

1do8C01TYR  112;LYS  183;ASP  279
GLU  255;ASP  256;ASP  279(Divalent metal binding)

1do8D01TYR  112;LYS  183;ASP  279
GLU  255;ASP  256;ASP  279(Divalent metal binding)

1efkA01TYR  112;LYS  183;ASP  279
GLU  255;ASP  256;ASP  279(Divalent metal binding)

1efkB01TYR  112;LYS  183;ASP  279
GLU  255;ASP  256;ASP  279(Divalent metal binding)

1efkC01TYR  112;LYS  183;ASP  279
GLU  255;ASP  256;ASP  279(Divalent metal binding)

1efkD01TYR  112;LYS  183;ASP  279
GLU  255;ASP  256;ASP  279(Divalent metal binding)

1eflA01TYR  112;LYS  183;ASP  279
GLU  255;ASP  256;ASP  279(Divalent metal binding)

1eflB01TYR  112;LYS  183;ASP  279
GLU  255;ASP  256;ASP  279(Divalent metal binding)

1eflC01TYR  112;LYS  183;ASP  279
GLU  255;ASP  256;ASP  279(Divalent metal binding)

1eflD01TYR  112;LYS  183;ASP  279
GLU  255;ASP  256;ASP  279(Divalent metal binding)

1gz3A01TYR  112;LYS  183;ASP  279
GLU  255;ASP  256;ASP  279(Divalent metal binding)
mutant R189Q
1gz3B01TYR  112;LYS  183;ASP  279
GLU  255;ASP  256;ASP  279(Divalent metal binding)
mutant R189Q
1gz3C01TYR  112;LYS  183;ASP  279
GLU  255;ASP  256;ASP  279(Divalent metal binding)
mutant R189Q
1gz3D01TYR  112;LYS  183;ASP  279
GLU  255;ASP  256;ASP  279(Divalent metal binding)
mutant R189Q
1gz4A01TYR  112;LYS  183;ASP  279
GLU  255;ASP  256;ASP  279(Divalent metal binding)

1gz4B01TYR  112;LYS  183;ASP  279
GLU  255;ASP  256;ASP  279(Divalent metal binding)

1gz4C01TYR  112;LYS  183;ASP  279
GLU  255;ASP  256;ASP  279(Divalent metal binding)

1gz4D01TYR  112;LYS  183;ASP  279
GLU  255;ASP  256;ASP  279(Divalent metal binding)

1pj2A01TYR  112;LYS  183;ASP  279
GLU  255;ASP  256;ASP  279(Divalent metal binding)

1pj2B01TYR 1112;LYS 1183;ASP 1279
GLU 1255;ASP 1256;ASP 1279(Divalent metal binding)

1pj2C01TYR 2112;LYS 2183;ASP 2279
GLU 2255;ASP 2256;ASP 2279(Divalent metal binding)

1pj2D01TYR 3112;LYS 3183;ASP 3279
GLU 3255;ASP 3256;ASP 3279(Divalent metal binding)

1pj3A01TYR  112;LYS  183;ASP  279
GLU  255;ASP  256;ASP  279(Divalent metal binding)

1pj3B01TYR 1112;LYS 1183;ASP 1279
GLU 1255;ASP 1256;ASP 1279(Divalent metal binding)

1pj3C01TYR 2112;LYS 2183;ASP 2279
GLU 2255;ASP 2256;ASP 2279(Divalent metal binding)

1pj3D01TYR 3112;LYS 3183;ASP 3279
GLU 3255;ASP 3256;ASP 3279(Divalent metal binding)

1pj4A01TYR  112;LYS  183;ASP  279
GLU  255;ASP  256;ASP  279(Divalent metal binding)

1pj4B01TYR 1112;LYS 1183;ASP 1279
GLU 1255;ASP 1256;ASP 1279(Divalent metal binding)

1pj4C01TYR 2112;LYS 2183;ASP 2279
GLU 2255;ASP 2256;ASP 2279(Divalent metal binding)

1pj4D01TYR 3112;LYS 3183;ASP 3279
GLU 3255;ASP 3256;ASP 3279(Divalent metal binding)

1pjlA01TYR  112;LYS  183;ASP  279
GLU  255;ASP  256;ASP  279(Divalent metal binding)

1pjlB01TYR 1112;LYS 1183;ASP 1279
GLU 1255;ASP 1256;ASP 1279(Divalent metal binding)

1pjlC01TYR 2112;LYS 2183;ASP 2279
GLU 2255;ASP 2256;ASP 2279(Divalent metal binding)

1pjlD01TYR 3112;LYS 3183;ASP 3279
GLU 3255;ASP 3256;ASP 3279(Divalent metal binding)

1pjlE01TYR 4112;LYS 4183;ASP 4279
GLU 4255;ASP 4256;ASP 4279(Divalent metal binding)

1pjlF01TYR 5112;LYS 5183;ASP 5279
GLU 5255;ASP 5256;ASP 5279(Divalent metal binding)

1pjlG01TYR 6112;LYS 6183;ASP 6279
GLU 6255;ASP 6256;ASP 6279(Divalent metal binding)

1pjlH01TYR 7112;LYS 7183;ASP 7279
GLU 7255;ASP 7256;ASP 7279(Divalent metal binding)

1qr6A01TYR  112;LYS  183;ASP  279
GLU  255;ASP  256;ASP  279(Divalent metal binding)

1qr6B01TYR 1112;LYS 1183;ASP 1279
GLU 1255;ASP 1256;ASP 1279(Divalent metal binding)

1llqA02


1llqB02


1o0sA02


1o0sB02


1do8A02


1do8B02


1do8C02


1do8D02


1efkA02


1efkB02


1efkC02


1efkD02


1eflA02


1eflB02


1eflC02


1eflD02


1gz3A02

mutant R523V, R556Q
1gz3B02

mutant R523V, R556Q
1gz3C02

mutant R523V, R556Q
1gz3D02

mutant R523V, R556Q
1gz4A02


1gz4B02


1gz4C02


1gz4D02


1pj2A02


1pj2B02


1pj2C02


1pj2D02


1pj3A02


1pj3B02


1pj3C02


1pj3D02


1pj4A02


1pj4B02


1pj4C02


1pj4D02


1pjlA02


1pjlB02


1pjlC02


1pjlD02


1pjlE02


1pjlF02


1pjlG02


1pjlH02


1qr6A02


1qr6B02



References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[6]Fig.1, p.10531-10532
[7]p.884-885
[9]Fig.3, p.254-255
[10]Scheme 2, p.6935-6937
[12]Scheme 1, p.38056-38058
[13]Fig.5, p.1145-1149
[15]Scheme 1

references
[1]
PubMed ID2043616
JournalBiochemistry
Year1991
Volume30
Pages5764-9
AuthorsGavva SR, Harris BG, Weiss PM, Cook PF
TitleModification of a thiol at the active site of the Ascaris suum NAD-malic enzyme results in changes in the rate-determining steps for oxidative decarboxylation of L-malate.
[2]
PubMed ID1993653
JournalJ Biol Chem
Year1991
Volume266
Pages2732-8
AuthorsMallick S, Harris BG, Cook PF
TitleKinetic mechanism of NAD:malic enzyme from Ascaris suum in the direction of reductive carboxylation.
[3]
PubMed ID8117666
JournalBiochemistry
Year1994
Volume33
Pages2096-103
AuthorsKarsten WE, Cook PF
TitleStepwise versus concerted oxidative decarboxylation catalyzed by malic enzyme: a reinvestigation.
[4]
PubMed ID7626027
JournalBiochem J
Year1995
Volume309
Pages607-11
AuthorsKochan Z, Karbowska J, Bukato G, Zydowo MM, Bertoli E, Tanfani F, Swierczynski J
TitleA comparison of the secondary structure of human brain mitochondrial and cytosolic 'malic' enzyme investigated by Fourier-transform infrared spectroscopy.
[5]
PubMed ID8844853
JournalProtein Sci
Year1996
Volume5
Pages1648-54
AuthorsTipton PA, Quinn TP, Peisach J, Cook PF
TitleRole of the divalent metal ion in the NAD:malic enzyme reaction: an ESEEM determination of the ground state conformation of malate in the E:Mn:malate complex.
[6]
PubMed ID10441149
JournalBiochemistry
Year1999
Volume38
Pages10527-32
AuthorsKarsten WE, Chooback L, Liu D, Hwang CC, Lynch C, Cook PF
TitleMapping the active site topography of the NAD-malic enzyme via alanine-scanning site-directed mutagenesis.
[7]
CommentsX-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
PubMed ID10467136
JournalStructure (Camb)
Year1999
Volume7
Pages877-89
AuthorsXu Y, Bhargava G, Wu H, Loeber G, Tong L
TitleCrystal structure of human mitochondrial NAD(P)(+)-dependent malic enzyme: a new class of oxidative decarboxylases.
Related PDB1qr6
Related Swiss-protP23368
[8]
CommentsX-ray crystallography
PubMed ID10913357
JournalBiochem Biophys Res Commun
Year2000
Volume274
Pages440-4
AuthorsYang Z, Batra R, Floyd DL, Hung HC, Chang GG, Tong L
TitlePotent and competitive inhibition of malic enzymes by lanthanide ions.
Related PDB1pjl
[9]
CommentsX-ray crystallography
PubMed ID10700286
JournalNat Struct Biol
Year2000
Volume7
Pages251-7
AuthorsYang Z, Floyd DL, Loeber G, Tong L
TitleStructure of a closed form of human malic enzyme and implications for catalytic mechanism.
Related PDB1do8,1efk,1efl
[10]
PubMed ID12033925
JournalBiochemistry
Year2002
Volume41
Pages6928-38
AuthorsColeman DE, Rao GS, Goldsmith EJ, Cook PF, Harris BG
TitleCrystal structure of the malic enzyme from Ascaris suum complexed with nicotinamide adenine dinucleotide at 2.3 A resolution.
Related PDB1llq
[11]
CommentsX-ray crystallography
PubMed ID12121650
JournalStructure (Camb)
Year2002
Volume10
Pages951-60
AuthorsYang Z, Lanks CW, Tong L
TitleMolecular mechanism for the regulation of human mitochondrial NAD(P)+-dependent malic enzyme by ATP and fumarate.
Related PDB1gz3,1gz4
[12]
PubMed ID12853453
JournalJ Biol Chem
Year2003
Volume278
Pages38051-8
AuthorsRao GS, Coleman DE, Karsten WE, Cook PF, Harris BG
TitleCrystallographic studies on Ascaris suum NAD-malic enzyme bound to reduced cofactor and identification of an effector site.
Related PDB1o0s
[13]
CommentsX-ray crystallography
PubMed ID12962632
JournalStructure (Camb)
Year2003
Volume11
Pages1141-50
AuthorsTao X, Yang Z, Tong L
TitleCrystal structures of substrate complexes of malic enzyme and insights into the catalytic mechanism.
Related PDB1pj2,1pj3,1pj4
[14]
PubMed ID15182181
JournalBiochemistry
Year2004
Volume43
Pages7382-90
AuthorsHsu WC, Hung HC, Tong L, Chang GG
TitleDual functional roles of ATP in the human mitochondrial malic enzyme.
[15]
PubMed ID14747989
JournalProteins
Year2004
Volume54
Pages404-11
AuthorsKuo CW, Hung HC, Tong L, Chang GG
TitleMetal-Induced reversible structural interconversion of human mitochondrial NAD(P)+-dependent malic enzyme.

comments
There are several types of malate deydrogenases.
1.1.1.37: Malate dehydrogenase / bacteria, rat, porcine
1.1.1.38: Malate dehydrogenase (oxaloacetate decarboxylating) / Human, Ascaris suum
1.1.1.39: Malate dehydrogenase (decarboxylating)
1.1.1.82: Malate dehydrogenase (NADP+) / Archaea, plant
1.1.1.40: Malate dehydrogenase (oxaloacetate decarboxylating) (NADP+) / pigeon
1.1.1.83: D-malate dehydrogenase (decarboxylating)
This enzyme catalyzes the following reactions:
(A) Hydride transfer from substrate, (S)-Malate, to NAD+, giving oxaloacetate and NADH:
(B) Eliminative double-bond formation; Elimination of CO2 from oxaloacetate, giving enolpyruvate:
(C) Isomerization (shift of double-bond position; from C=C-O to C-C=O):

createdupdated
2004-12-072009-02-26


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)

© Computational Biology Research Center, AIST, 2004 All Rights Reserved.