D00032
type: Enzyme
cath: Leucine Dehydrogenase; Chain A, domain 1
cath: Rossmann fold
ec: https://purl.uniprot.org/enzyme/1.4.1.3
uniprot: P80319
uniprot: P96110
kegg enzyme: glutamate dehydrogenase [NAD(P)+]
kegg enzyme: glutamic dehydrogenase
kegg pathway: Glutamate metabolism
kegg pathway: Arginine and proline metabolism
kegg pathway: D-Glutamine and D-glutamate metabolism
kegg pathway: Nitrogen metabolism
kegg substrate: NAD+
kegg substrate: NADP+
kegg substrate: L-Glutamate
kegg substrate: H2O
kegg product: NADH
kegg product: NADPH
kegg product: 2-Oxoglutarate
kegg product: NH3
kegg product: H+
pdb: 1b26A01
pdb: 1b26B01
pdb: 1b26C01
pdb: 1b26D01
pdb: 1b26E01
pdb: 1b26F01
pdb: 1bvuA01
pdb: 1bvuB01
pdb: 1bvuC01
pdb: 1bvuD01
pdb: 1bvuE01
pdb: 1bvuF01
pdb: 1gtmA01
pdb: 1gtmB01
pdb: 1gtmC01
pdb: 2tmgA01
pdb: 2tmgB01
pdb: 2tmgC01
pdb: 2tmgD01
pdb: 2tmgE01
pdb: 2tmgF01
pdb: 1b26A02
pdb: 1b26B02
pdb: 1b26C02
pdb: 1b26D02
pdb: 1b26E02
pdb: 1b26F02
pdb: 1bvuA02
pdb: 1bvuB02
pdb: 1bvuC02
pdb: 1bvuD02
pdb: 1bvuE02
pdb: 1bvuF02
pdb: 1gtmA02
pdb: 1gtmB02
pdb: 1gtmC02
pdb: 2tmgA02
pdb: 2tmgB02
pdb: 2tmgC02
pdb: 2tmgD02
pdb: 2tmgE02
pdb: 2tmgF02
pdb bound state: Unbound
  compound: NAD+
  pdb: 1b26A01
pdb bound state: Unbound
  compound: NAD+
  pdb: 1b26B01
pdb bound state: Unbound
  compound: NAD+
  pdb: 1b26C01
active site residues resources: P80319
active site residues resources: P96110
references: Characterization of an extremely thermostable glutamate dehydrogenase: a key enzyme in the primary metabolism of the hyperthermophilic archaebacterium, Pyrococcus furiosus.
references: Insights into thermal stability from a comparison of the glutamate dehydrogenases from Pyrococcus furiosus and Thermococcus litoralis.
references: The structure of Pyrococcus furiosus glutamate dehydrogenase reveals a key role for ion-pair networks in maintaining enzyme stability at extreme temperatures.
references: Re-activation of Clostridium symbiosum glutamate dehydrogenase from subunits denatured by urea.
references: Crystal structure of glutamate dehydrogenase from the hyperthermophilic eubacterium Thermotoga maritima at 3.0 A resolution.
references: Enzyme activity below the dynamical transition at 220 K.
references: Engineering activity and stability of Thermotoga maritima glutamate dehydrogenase. I. Introduction of a six-residue ion-pair network in the hinge region.
references: Amino acid residues involved in the catalytic mechanism of NAD-dependent glutamate dehydrogenase from Halobacterium salinarum.
references: Engineering activity and stability of Thermotoga maritima glutamate dehydrogenase. II: construction of a 16-residue ion-pair network at the subunit interface.
references: Structure determination of the glutamate dehydrogenase from the hyperthermophile Thermococcus litoralis and its comparison with that from Pyrococcus furiosus.
references: A new class of glutamate dehydrogenases (GDH). Biochemical and genetic characterization of the first member, the AMP-requiring NAD-specific GDH of Streptomyces clavuligerus.
comment: This enzyme catalyzes three reactions, dehydrogenation, addition of hydroxyl group to double-bond and elimination accompanied by double-bond formation (see T00010; homologous enzyme).

Leucine Dehydrogenase; Chain A, domain 1
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/3.40.192.10
catalytic domain: index.html

Rossmann fold
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/3.40.50.720

Glutamate metabolism
type: KeggPathway
references: KEGG:MAP00251

Arginine and proline metabolism
type: KeggPathway
references: KEGG:MAP00330

D-Glutamine and D-glutamate metabolism
type: KeggPathway
references: KEGG:MAP00471

Nitrogen metabolism
type: KeggPathway
references: KEGG:MAP00910

NAD+
type: KeggSubstrate
references: KEGG:C00003
compound type: amide group
compound type: amine group
compound type: nucleotide
references: CHEBI:15846
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

NADP+
type: KeggSubstrate
references: KEGG:C00006
compound type: amide group
compound type: amine group
compound type: nucleotide
references: CHEBI:18009
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

L-Glutamate
type: KeggSubstrate
references: KEGG:C00025
compound type: amino acids
compound type: carboxyl group
references: CHEBI:16015
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

H2O
type: KeggSubstrate
references: KEGG:C00001
compound type: H2O
references: CHEBI:15377
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

NADH
type: KeggProduct
references: KEGG:C00004
compound type: amide group
compound type: amine group
compound type: nucleotide
references: CHEBI:16908
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

NADPH
type: KeggProduct
references: KEGG:C00005
compound type: amide group
compound type: amine group
compound type: nucleotide
references: CHEBI:16474
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

2-Oxoglutarate
type: KeggProduct
references: KEGG:C00026
compound type: carbohydrate
compound type: carboxyl group
references: CHEBI:30915
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

NH3
type: KeggProduct
references: KEGG:C00014
compound type: amine group
compound type: organic ion
references: CHEBI:16134
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

H+
type: KeggProduct
references: KEGG:C00080
compound type: others
references: CHEBI:15378
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

1b26A01
type: Pdb
references: 1b26
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1b26
catalytic residue: LYS 104

1b26B01
type: Pdb
references: 1b26
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1b26
catalytic residue: LYS 104

1b26C01
type: Pdb
references: 1b26
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1b26
catalytic residue: LYS 104

1b26D01
type: Pdb
references: 1b26
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1b26
catalytic residue: LYS 104

1b26E01
type: Pdb
references: 1b26
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1b26
catalytic residue: LYS 104

1b26F01
type: Pdb
references: 1b26
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1b26
catalytic residue: LYS 104

1bvuA01
type: Pdb
references: 1bvu
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1bvu
catalytic residue: LYS 104

1bvuB01
type: Pdb
references: 1bvu
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1bvu
catalytic residue: LYS 104

1bvuC01
type: Pdb
references: 1bvu
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1bvu
catalytic residue: LYS 104

1bvuD01
type: Pdb
references: 1bvu
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1bvu
catalytic residue: LYS 104

1bvuE01
type: Pdb
references: 1bvu
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1bvu
catalytic residue: LYS 104

1bvuF01
type: Pdb
references: 1bvu
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1bvu
catalytic residue: LYS 104

1gtmA01
type: Pdb
references: 1gtm
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1gtm
catalytic residue: LYS 104

1gtmB01
type: Pdb
references: 1gtm
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1gtm
catalytic residue: LYS 104

1gtmC01
type: Pdb
references: 1gtm
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1gtm
catalytic residue: LYS 104

2tmgA01
type: Pdb
references: 2tmg
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2tmg
catalytic residue: LYS 104
comment: mutant N117R;S128R;T158E;S160E

2tmgB01
type: Pdb
references: 2tmg
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2tmg
catalytic residue: LYS 104
comment: mutant N117R;S128R;T158E;S160E

2tmgC01
type: Pdb
references: 2tmg
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2tmg
catalytic residue: LYS 104
comment: mutant N117R;S128R;T158E;S160E

2tmgD01
type: Pdb
references: 2tmg
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2tmg
catalytic residue: LYS 104
comment: mutant N117R;S128R;T158E;S160E

2tmgE01
type: Pdb
references: 2tmg
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2tmg
catalytic residue: LYS 104
comment: mutant N117R;S128R;T158E;S160E

2tmgF01
type: Pdb
references: 2tmg
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2tmg
catalytic residue: LYS 104
comment: mutant N117R;S128R;T158E;S160E

Characterization of an extremely thermostable glutamate dehydrogenase: a key enzyme in the primary metabolism of the hyperthermophilic archaebacterium, Pyrococcus furiosus.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/1576153
journal: Biochim Biophys Acta
volume: 1120
pages: 267-72
published year: 1992
authors:
  item: Robb FT
  item: Park JB
  item: Adams MW

Insights into thermal stability from a comparison of the glutamate dehydrogenases from Pyrococcus furiosus and Thermococcus litoralis.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/7758464
journal: Eur J Biochem
volume: 229
pages: 688-95
published year: 1995
authors:
  item: Britton KL
  item: Baker PJ
  item: Borges KM
  item: Engel PC
  item: Pasquo A
  item: Rice DW
  item: Robb FT
  item: Scandurra R
  item: Stillman TJ
  item: Yip KS

The structure of Pyrococcus furiosus glutamate dehydrogenase reveals a key role for ion-pair networks in maintaining enzyme stability at extreme temperatures.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS)
medline id: 96164432
references: http://www.ncbi.nlm.nih.gov/pubmed/8591026
journal: Structure
volume: 3
pages: 1147-58
published year: 1995
authors:
  item: Yip KS
  item: Stillman TJ
  item: Britton KL
  item: Artymiuk PJ
  item: Baker PJ
  item: Sedelnikova SE
  item: Engel PC
  item: Pasquo A
  item: Chiaraluce R
  item: Consalvi V
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P80319

Re-activation of Clostridium symbiosum glutamate dehydrogenase from subunits denatured by urea.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9307012
journal: Biochem J
volume: 326
pages: 649-55
published year: 1997
authors:
  item: Aghajanian S
  item: Engel PC

Crystal structure of glutamate dehydrogenase from the hyperthermophilic eubacterium Thermotoga maritima at 3.0 A resolution.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS)
medline id: 97280794
references: http://www.ncbi.nlm.nih.gov/pubmed/9135121
journal: J Mol Biol
volume: 267
pages: 916-32
published year: 1997
authors:
  item: Knapp S
  item: de Vos WM
  item: Rice D
  item: Ladenstein R
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P96110

Enzyme activity below the dynamical transition at 220 K.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9788945
journal: Biophys J
volume: 75
pages: 2504-7
published year: 1998
authors:
  item: Daniel RM
  item: Smith JC
  item: Ferrand M
  item: Hery S
  item: Dunn R
  item: Finney JL

Engineering activity and stability of Thermotoga maritima glutamate dehydrogenase. I. Introduction of a six-residue ion-pair network in the hinge region.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS)
medline id: 98319860
references: http://www.ncbi.nlm.nih.gov/pubmed/9654452
journal: J Mol Biol
volume: 280
pages: 287-96
published year: 1998
authors:
  item: Lebbink JH
  item: Knapp S
  item: van der Oost J
  item: Rice D
  item: Ladenstein R
  item: de Vos WM
references: P96110

Amino acid residues involved in the catalytic mechanism of NAD-dependent glutamate dehydrogenase from Halobacterium salinarum.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10076069
journal: Biochim Biophys Acta
volume: 1426
pages: 513-25
published year: 1999
authors:
  item: Perez-Pomares F
  item: Ferrer J
  item: Camacho M
  item: Pire C
  item: LLorca F
  item: Bonete MJ

Engineering activity and stability of Thermotoga maritima glutamate dehydrogenase. II: construction of a 16-residue ion-pair network at the subunit interface.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS)
medline id: 99296634
references: http://www.ncbi.nlm.nih.gov/pubmed/10366510
journal: J Mol Biol
volume: 289
pages: 357-69
published year: 1999
authors:
  item: Lebbink JH
  item: Knapp S
  item: van der Oost J
  item: Rice D
  item: Ladenstein R
  item: de Vos WM
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P96110

Structure determination of the glutamate dehydrogenase from the hyperthermophile Thermococcus litoralis and its comparison with that from Pyrococcus furiosus.
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/10547290
journal: J Mol Biol
volume: 293
pages: 1121-32
published year: 1999
authors:
  item: Britton KL
  item: Yip KS
  item: Sedelnikova SE
  item: Stillman TJ
  item: Adams MW
  item: Ma K
  item: Maeder DL
  item: Robb FT
  item: Tolliday N
  item: Vetriani C
  item: Rice DW
  item: Baker PJ
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

A new class of glutamate dehydrogenases (GDH). Biochemical and genetic characterization of the first member, the AMP-requiring NAD-specific GDH of Streptomyces clavuligerus.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10924516
journal: J Biol Chem
volume: 275
pages: 39529-42
published year: 2000
authors:
  item: Minambres B
  item: Olivera ER
  item: Jensen RA
  item: Luengo JM

ReferenceForCatalyticMechanism
reference index: 8
reference section: Fig.6, p.524
reference step: 3