DB code: D00032

CATH domain 3.40.192.10 : Leucine Dehydrogenase; Chain A, domain 1 Catalytic domain
3.40.50.720 : Rossmann fold
E.C. 1.4.1.3
CSA
M-CSA
MACiE

CATH domain Related DB codes (homologues)
3.40.192.10 : Leucine Dehydrogenase; Chain A, domain 1 D00458 D00033 D00035 D00605 D00845 D00857 D00858 M00210 T00010 T00011 T00414
3.40.50.720 : Rossmann fold S00543 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 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

Uniprot Enzyme Name
UniprotKB Protein name Synonyms RefSeq Pfam
P80319 Glutamate dehydrogenase
GDH
EC 1.4.1.3
NP_579331.1 (Protein)
NC_003413.1 (DNA/RNA sequence)
PF00208 (ELFV_dehydrog)
PF02812 (ELFV_dehydrog_N)
[Graphical View]
P96110 Glutamate dehydrogenase
GDH
EC 1.4.1.3
NP_228821.1 (Protein)
NC_000853.1 (DNA/RNA sequence)
PF00208 (ELFV_dehydrog)
PF02812 (ELFV_dehydrog_N)
[Graphical View]

KEGG enzyme name
glutamate dehydrogenase [NAD(P)+]
glutamic dehydrogenase
glutamate dehydrogenase [NAD(P)+]

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P80319 DHE3_PYRFU L-glutamate + H(2)O + NAD(P)(+) = 2- oxoglutarate + NH(3) + NAD(P)H. Homohexamer. Cytoplasm.
P96110 DHE3_THEMA L-glutamate + H(2)O + NAD(P)(+) = 2- oxoglutarate + NH(3) + NAD(P)H. Homohexamer.

KEGG Pathways
Map code Pathways E.C.
MAP00251 Glutamate metabolism
MAP00330 Arginine and proline metabolism
MAP00471 D-Glutamine and D-glutamate metabolism
MAP00910 Nitrogen metabolism

Compound table
Substrates Products Intermediates
KEGG-id C00003 C00006 C00025 C00001 C00004 C00005 C00026 C00014 C00080
E.C.
Compound NAD+ NADP+ L-Glutamate H2O NADH NADPH 2-Oxoglutarate NH3 H+
Type amide group,amine group,nucleotide amide group,amine group,nucleotide amino acids,carboxyl group H2O amide group,amine group,nucleotide amide group,amine group,nucleotide carbohydrate,carboxyl group amine group,organic ion others
ChEBI 15846
 15846
 		18009
 18009
 		16015
 16015
 		15377
 15377
 		16908
 16908
 		16474
 16474
 		30915
 30915
 		16134
 16134
 		15378
 15378
PubChem 5893
 5893
 		5886
 5886
 		33032
 44272391
 88747398
 33032
 44272391
 88747398
 		22247451
 962
 22247451
 962
 		439153
 439153
 		5884
 5884
 		51
 51
 		222
 222
 		1038
 1038
1b26A01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1b26B01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1b26C01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1b26D01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1b26E01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1b26F01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1bvuA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1bvuB01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1bvuC01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1bvuD01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1bvuE01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1bvuF01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1gtmA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1gtmB01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1gtmC01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound
2tmgA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound
2tmgB01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound
2tmgC01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound
2tmgD01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound
2tmgE01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound
2tmgF01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1b26A02 Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1b26B02 Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1b26C02 Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1b26D02 Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1b26E02 Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1b26F02 Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1bvuA02 Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1bvuB02 Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1bvuC02 Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1bvuD02 Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1bvuE02 Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1bvuF02 Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1gtmA02 Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1gtmB02 Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1gtmC02 Unbound Unbound Unbound Unbound Unbound Unbound Unbound
2tmgA02 Unbound Unbound Unbound Unbound Unbound Unbound Unbound
2tmgB02 Unbound Unbound Unbound Unbound Unbound Unbound Unbound
2tmgC02 Unbound Unbound Unbound Unbound Unbound Unbound Unbound
2tmgD02 Unbound Unbound Unbound Unbound Unbound Unbound Unbound
2tmgE02 Unbound Unbound Unbound Unbound Unbound Unbound Unbound
2tmgF02 Unbound Unbound Unbound Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
Swiss-prot; P80319, P96110

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1b26A01 LYS 104
1b26B01 LYS 104
1b26C01 LYS 104
1b26D01 LYS 104
1b26E01 LYS 104
1b26F01 LYS 104
1bvuA01 LYS 104
1bvuB01 LYS 104
1bvuC01 LYS 104
1bvuD01 LYS 104
1bvuE01 LYS 104
1bvuF01 LYS 104
1gtmA01 LYS 104
1gtmB01 LYS 104
1gtmC01 LYS 104
2tmgA01 LYS 104 mutant N117R;S128R;T158E;S160E
2tmgB01 LYS 104 mutant N117R;S128R;T158E;S160E
2tmgC01 LYS 104 mutant N117R;S128R;T158E;S160E
2tmgD01 LYS 104 mutant N117R;S128R;T158E;S160E
2tmgE01 LYS 104 mutant N117R;S128R;T158E;S160E
2tmgF01 LYS 104 mutant N117R;S128R;T158E;S160E
1b26A02
1b26B02
1b26C02
1b26D02
1b26E02
1b26F02
1bvuA02
1bvuB02
1bvuC02
1bvuD02
1bvuE02
1bvuF02
1gtmA02
1gtmB02
1gtmC02
2tmgA02
2tmgB02
2tmgC02
2tmgD02
2tmgE02
2tmgF02

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[8]
Fig.6, p.524 3

References
[1]
Resource
Comments
Medline ID
PubMed ID 1576153
Journal Biochim Biophys Acta
Year 1992
Volume 1120
Pages 267-72
Authors Robb FT, Park JB, Adams MW
Title Characterization of an extremely thermostable glutamate dehydrogenase: a key enzyme in the primary metabolism of the hyperthermophilic archaebacterium, Pyrococcus furiosus.
Related PDB
Related UniProtKB
[2]
Resource
Comments
Medline ID
PubMed ID 7758464
Journal Eur J Biochem
Year 1995
Volume 229
Pages 688-95
Authors Britton KL, Baker PJ, Borges KM, Engel PC, Pasquo A, Rice DW, Robb FT, Scandurra R, Stillman TJ, Yip KS
Title Insights into thermal stability from a comparison of the glutamate dehydrogenases from Pyrococcus furiosus and Thermococcus litoralis.
Related PDB
Related UniProtKB
[3]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS)
Medline ID 96164432
PubMed ID 8591026
Journal Structure
Year 1995
Volume 3
Pages 1147-58
Authors Yip KS, Stillman TJ, Britton KL, Artymiuk PJ, Baker PJ, Sedelnikova SE, Engel PC, Pasquo A, Chiaraluce R, Consalvi V
Title The structure of Pyrococcus furiosus glutamate dehydrogenase reveals a key role for ion-pair networks in maintaining enzyme stability at extreme temperatures.
Related PDB 1gtm
Related UniProtKB P80319
[4]
Resource
Comments
Medline ID
PubMed ID 9307012
Journal Biochem J
Year 1997
Volume 326
Pages 649-55
Authors Aghajanian S, Engel PC
Title Re-activation of Clostridium symbiosum glutamate dehydrogenase from subunits denatured by urea.
Related PDB
Related UniProtKB
[5]
Resource
Comments X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS)
Medline ID 97280794
PubMed ID 9135121
Journal J Mol Biol
Year 1997
Volume 267
Pages 916-32
Authors Knapp S, de Vos WM, Rice D, Ladenstein R
Title Crystal structure of glutamate dehydrogenase from the hyperthermophilic eubacterium Thermotoga maritima at 3.0 A resolution.
Related PDB 1b26
Related UniProtKB P96110
[6]
Resource
Comments
Medline ID
PubMed ID 9788945
Journal Biophys J
Year 1998
Volume 75
Pages 2504-7
Authors Daniel RM, Smith JC, Ferrand M, Hery S, Dunn R, Finney JL
Title Enzyme activity below the dynamical transition at 220 K.
Related PDB
Related UniProtKB
[7]
Resource
Comments X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS)
Medline ID 98319860
PubMed ID 9654452
Journal J Mol Biol
Year 1998
Volume 280
Pages 287-96
Authors Lebbink JH, Knapp S, van der Oost J, Rice D, Ladenstein R, de Vos WM
Title Engineering activity and stability of Thermotoga maritima glutamate dehydrogenase. I. Introduction of a six-residue ion-pair network in the hinge region.
Related PDB
Related UniProtKB P96110
[8]
Resource
Comments
Medline ID
PubMed ID 10076069
Journal Biochim Biophys Acta
Year 1999
Volume 1426
Pages 513-25
Authors Perez-Pomares F, Ferrer J, Camacho M, Pire C, LLorca F, Bonete MJ
Title Amino acid residues involved in the catalytic mechanism of NAD-dependent glutamate dehydrogenase from Halobacterium salinarum.
Related PDB
Related UniProtKB
[9]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS)
Medline ID 99296634
PubMed ID 10366510
Journal J Mol Biol
Year 1999
Volume 289
Pages 357-69
Authors Lebbink JH, Knapp S, van der Oost J, Rice D, Ladenstein R, de Vos WM
Title Engineering activity and stability of Thermotoga maritima glutamate dehydrogenase. II: construction of a 16-residue ion-pair network at the subunit interface.
Related PDB 2tmg
Related UniProtKB P96110
[10]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 10547290
Journal J Mol Biol
Year 1999
Volume 293
Pages 1121-32
Authors Britton KL, Yip KS, Sedelnikova SE, Stillman TJ, Adams MW, Ma K, Maeder DL, Robb FT, Tolliday N, Vetriani C, Rice DW, Baker PJ
Title Structure determination of the glutamate dehydrogenase from the hyperthermophile Thermococcus litoralis and its comparison with that from Pyrococcus furiosus.
Related PDB 1bvu
Related UniProtKB
[11]
Resource
Comments
Medline ID
PubMed ID 10924516
Journal J Biol Chem
Year 2000
Volume 275
Pages 39529-42
Authors Minambres B, Olivera ER, Jensen RA, Luengo JM
Title A new class of glutamate dehydrogenases (GDH). Biochemical and genetic characterization of the first member, the AMP-requiring NAD-specific GDH of Streptomyces clavuligerus.
Related PDB
Related UniProtKB

Comments
This enzyme catalyzes three reactions, dehydrogenation, addition of hydroxyl group to double-bond and elimination accompanied by double-bond formation (see T00010; homologous enzyme).

Created Updated
2004-04-01 2009-02-26