EzCatDB: T00010
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DB codeT00010
CATH domainDomain 13.40.50.720 : Rossmann fold
Domain 23.40.192.10 : Leucine Dehydrogenase; Chain A, domain 1Catalytic domain
Domain 31.10.285.10 : Glutamate Dehydrogenase; Chain A, domain 3
E.C.1.4.1.2
CSA1hrd

CATH domainRelated DB codes (homologues)
3.40.192.10 : Leucine Dehydrogenase; Chain A, domain 1D00458,D00032,D00033,D00035,D00605,D00845,D00857,D00858,M00210,T00011,T00414
3.40.50.720 : Rossmann foldS00543,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,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,T00011,T00015,T00227,T00247,T00408,T00414,D00827,D00262,D00274,D00275,M00035,T00109

Enzyme Name
UniProtKBKEGG

P24295
Protein nameNAD-specific glutamate dehydrogenaseglutamate dehydrogenase
glutamic dehydrogenase
glutamate dehydrogenase (NAD+)
glutamate oxidoreductase
glutamic acid dehydrogenase
L-glutamate dehydrogenase
NAD+-dependent glutamate dehydrogenase
NAD+-dependent glutamic dehydrogenase
NAD+-glutamate dehydrogenase
NAD+-linked glutamate dehydrogenase
NAD+-linked glutamic dehydrogenase
NAD+-specific glutamic dehydrogenase
NAD+-specific glutamate dehydrogenase
NAD+:glutamate oxidoreductase
NADH-linked glutamate dehydrogenase
SynonymsNAD-GDH
EC 1.4.1.2
PfamPF00208 (ELFV_dehydrog)
PF02812 (ELFV_dehydrog_N)
[Graphical view]

KEGG pathways
MAP codePathways
MAP00251Glutamate metabolism
MAP00910Nitrogen metabolism

UniProtKB:Accession NumberP24295
Entry nameDHE2_CLOSY
ActivityL-glutamate + H(2)O + NAD(+) = 2-oxoglutarate + NH(3) + NADH.
SubunitHomohexamer.
Subcellular location
Cofactor

Compound table: links to PDB-related databases & PoSSuM

SubstratesProducts
KEGG-idC00025C00001C00003C00026C00014C00004C00080
CompoundL-GlutamateH2ONAD+2-OxoglutarateNH3NADHH+
Typeamino acids,carboxyl groupH2Oamide group,amine group,nucleotidecarbohydrate,carboxyl groupamine group,organic ionamide group,amine group,nucleotideothers
ChEBI16015
15377
15846
30915
16134
16908
15378
PubChem88747398
44272391
33032
962
22247451
5893
51
222
439153
1038
               
1aupA01Unbound UnboundUnboundUnboundUnbound 
1bgvA01Unbound UnboundUnboundUnboundUnbound 
1hrdA01Unbound UnboundUnboundUnboundUnbound 
1hrdB01Unbound UnboundUnboundUnboundUnbound 
1hrdC01Unbound UnboundUnboundUnboundUnbound 
1k89A01Unbound UnboundUnboundUnboundUnbound 
1aupA02Unbound UnboundUnboundUnboundUnbound 
1bgvA02Bound:GLU UnboundUnboundUnboundUnbound 
1hrdA02Unbound UnboundUnboundUnboundUnbound 
1hrdB02Unbound UnboundUnboundUnboundUnbound 
1hrdC02Unbound UnboundUnboundUnboundUnbound 
1k89A02Unbound UnboundUnboundUnboundUnbound 
1aupA03Unbound UnboundUnboundUnboundUnbound 
1bgvA03Unbound UnboundUnboundUnboundUnbound 
1hrdA03Unbound UnboundUnboundUnboundUnbound 
1hrdB03Unbound UnboundUnboundUnboundUnbound 
1hrdC03Unbound UnboundUnboundUnboundUnbound 
1k89A03Unbound UnboundUnboundUnboundUnbound 

Active-site residues
resource
Swiss-prot;P24295
pdbCatalytic residuescomment
          
1aupA01 
 
1bgvA01 
 
1hrdA01 
 
1hrdB01 
 
1hrdC01 
 
1k89A01 
 
1aupA02LYS 125;ASP 165
mutant K89I
1bgvA02LYS 125;ASP 165
 
1hrdA02LYS 125;ASP 165
 
1hrdB02LYS 125;ASP 165
 
1hrdC02LYS 125;ASP 165
 
1k89A02LYS 125;ASP 165
mutant K89I
1aupA03 
 
1bgvA03 
 
1hrdA03 
 
1hrdB03 
 
1hrdC03 
 
1k89A03 
 

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[7]Fig.5, p.1136-11383
[15]Fig.6, p.524
[21]


references
[1]
PubMed ID3981633
JournalJ Mol Biol
Year1985
Volume181
Pages147-9
AuthorsRice DW, Hornby DP, Engel PC
TitleCrystallization of an NAD+-dependent glutamate dehydrogenase from Clostridium symbiosum.
[2]
PubMed ID3593276
JournalBiochem J
Year1987
Volume242
Pages789-95
AuthorsRice DW, Baker PJ, Farrants GW, Hornby DP
TitleThe crystal structure of glutamate dehydrogenase from Clostridium symbiosum at 0.6 nm resolution.
[3]
PubMed ID1764463
JournalBiochim Biophys Acta
Year1991
Volume1115
Pages123-30
AuthorsSyed SE, Engel PC, Parker DM
TitleFunctional studies of a glutamate dehydrogenase with known three-dimensional structure: steady-state kinetics of the forward and reverse reactions catalysed by the NAD(+)-dependent glutamate dehydrogenase of Clostridium symbiosum.
[4]
PubMed ID1633808
JournalEur J Biochem
Year1992
Volume207
Pages533-40
AuthorsLilley KS, Engel PC
TitleThe essential active-site lysines of clostridial glutamate dehydrogenase. A study with pyridoxal-5'-phosphate.
[5]
PubMed ID1349042
JournalJ Mol Biol
Year1992
Volume224
Pages1181-4
AuthorsStillman TJ, Baker PJ, Britton KL, Rice DW, Rodgers HF
TitleEffect of additives on the crystallization of glutamate dehydrogenase from Clostridium symbiosum. Evidence for a ligand-induced conformational change.
[6]
CommentsX-RAY CRYSTALLOGRAPHY (1.96 ANGSTROMS).
Medline ID92204934
PubMed ID1553382
JournalProteins
Year1992
Volume12
Pages75-86
AuthorsBaker PJ, Britton KL, Engel PC, Farrants GW, Lilley KS, Rice DW, Stillman TJ
TitleSubunit assembly and active site location in the structure of glutamate dehydrogenase.
Related UniProtKBP24295
[7]
CommentsX-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
Medline ID94087726
PubMed ID8263917
JournalJ Mol Biol
Year1993
Volume234
Pages1131-9
AuthorsStillman TJ, Baker PJ, Britton KL, Rice DW
TitleConformational flexibility in glutamate dehydrogenase. Role of water in substrate recognition and catalysis.
Related PDB1bgv
Related UniProtKBP24295
[8]
PubMed ID8263939
JournalJ Mol Biol
Year1993
Volume234
Pages938-45
AuthorsBritton KL, Baker PJ, Engel PC, Rice DW, Stillman TJ
TitleEvolution of substrate diversity in the superfamily of amino acid dehydrogenases. Prospects for rational chiral synthesis.
[9]
PubMed ID8129708
JournalBiochem J
Year1994
Volume298
Pages107-13
AuthorsSyed SE, Hornby DP, Brown PE, Fitton JE, Engel PC
TitleSite and significance of chemically modifiable cysteine residues in glutamate dehydrogenase of Clostridium symbiosum and the use of protection studies to measure coenzyme binding.
[10]
PubMed ID8037659
JournalBiochem J
Year1994
Volume301
Pages13-6
AuthorsDean JL, Wang XG, Teller JK, Waugh ML, Britton KL, Baker PJ, Stillman TJ, Martin SR, Rice DW, Engel PC
TitleThe catalytic role of aspartate in the active site of glutamate dehydrogenase.
[11]
CommentsX-ray crystallography
PubMed ID8591026
JournalStructure
Year1995
Volume3
Pages1147-58
AuthorsYip KS, Stillman TJ, Britton KL, Artymiuk PJ, Baker PJ, Sedelnikova SE, Engel PC, Pasquo A, Chiaraluce R, Consalvi V
TitleThe structure of Pyrococcus furiosus glutamate dehydrogenase reveals a key role for ion-pair networks in maintaining enzyme stability at extreme temperatures.
Related PDB1hrd
[12]
CommentsX-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
Medline ID98070235
PubMed ID9405044
JournalBiochemistry
Year1997
Volume36
Pages16109-15
AuthorsBaker PJ, Waugh ML, Wang XG, Stillman TJ, Turnbull AP, Engel PC, Rice DW
TitleDeterminants of substrate specificity in the superfamily of amino acid dehydrogenases.
Related PDB1aup
Related UniProtKBP24295
[13]
PubMed ID9188163
JournalEur Biophys J
Year1997
Volume25
Pages417-22
AuthorsDean JL, Colfen H, Harding SE, Rice DW, Engel PC
TitleAlteration of the quaternary structure of glutamate dehydrogenase from Clostridium symbiosum by a single mutation distant from the subunit interfaces.
[14]
PubMed ID10333502
JournalBiochem J
Year1999
Volume340
Pages555-60
AuthorsHayden BM, Dean JL, Martin SR, Engel PC
TitleChemical rescue of the catalytically disabled clostridial glutamate dehydrogenase mutant D165S by fluoride ion.
[15]
PubMed ID10076069
JournalBiochim Biophys Acta
Year1999
Volume1426
Pages513-25
AuthorsPerez-Pomares F, Ferrer J, Camacho M, Pire C, LLorca F, Bonete MJ
TitleAmino acid residues involved in the catalytic mechanism of NAD-dependent glutamate dehydrogenase from Halobacterium salinarum.
[16]
PubMed ID10607407
JournalBiochimie
Year1999
Volume81
Pages1123-9
AuthorsAhn JY, Choi S, Cho SW
TitleIdentification of lysine residue involved in inactivation of brain glutamate dehydrogenase isoproteins by o-phthalaldehyde.
[17]
CommentsX-ray crystallography
PubMed ID9878450
JournalJ Mol Biol
Year1999
Volume285
Pages875-85
AuthorsStillman TJ, Migueis AM, Wang XG, Baker PJ, Britton KL, Engel PC, Rice DW
TitleInsights into the mechanism of domain closure and substrate specificity of glutamate dehydrogenase from Clostridium symbiosum.
Related PDB1k89
[18]
PubMed ID10790778
JournalBioelectrochemistry
Year2000
Volume51
Pages35-9
AuthorsDai HC, Zhuang QK, Li NQ, Luo HX, Gao XX
TitleElectrochemical study of the effect of ADP and AMP on the kinetics of glutamate dehydrogenase.
[19]
PubMed ID10924516
JournalJ Biol Chem
Year2000
Volume275
Pages39529-42
AuthorsMinambres B, Olivera ER, Jensen RA, Luengo JM
TitleA new class of glutamate dehydrogenases (GDH). Biochemical and genetic characterization of the first member, the AMP-requiring NAD-specific GDH of Streptomyces clavuligerus.
[20]
PubMed ID11231268
JournalEur J Biochem
Year2001
Volume268
Pages1173-80
AuthorsHayden BM, Engel PC
TitleConstruction, separation and properties of hybrid hexamers of glutamate dehydrogenase in which five of the six subunits are contributed by the catalytically inert D165S.
[21]
PubMed ID12220195
JournalBiochemistry
Year2002
Volume41
Pages11284-93
AuthorsTally JF, Maniscalco SJ, Saha SK, Fisher HF
TitleDetection of multiple active site domain motions in transient-state component time courses of the Clostridium symbiosum L-glutamate dehydrogenase-catalyzed oxidative deamination reaction.

comments
This enzyme catalyzes three reactions, dehydrogenation, addition of hydroxyl group to double-bond and elimination accompanied by double-bond formation (see [7]).

createdupdated
2003-10-302009-02-26


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Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
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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)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2012 - March 2013)
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