DB code: T00011

CATH domain 1.10.287.140 : Helix Hairpins
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 D00032 D00033 D00035 D00605 D00845 D00857 D00858 M00210 T00010 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 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 T00015 T00227 T00247 T00408 T00414 D00827 D00262 D00274 D00275 M00035 T00109

Uniprot Enzyme Name
UniprotKB Protein name Synonyms RefSeq Pfam
P00366 Glutamate dehydrogenase 1, mitochondrial
GDH
EC 1.4.1.3
NP_872593.1 (Protein)
NM_182652.1 (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
P00366 DHE3_BOVIN L-glutamate + H(2)O + NAD(P)(+) = 2- oxoglutarate + NH(3) + NAD(P)H. Homohexamer. Mitochondrion matrix.

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 C00025 C00001 C00003 C00006 C00026 C00014 C00080 C00004 C00005
E.C.
Compound L-Glutamate H2O NAD+ NADP+ 2-Oxoglutarate NH3 H+ NADH NADPH
Type amino acids,carboxyl group H2O amide group,amine group,nucleotide amide group,amine group,nucleotide carbohydrate,carboxyl group amine group,organic ion others amide group,amine group,nucleotide amide group,amine group,nucleotide
ChEBI 16015
16015
15377
15377
15846
15846
18009
18009
30915
30915
16134
16134
15378
15378
16908
16908
16474
16474
PubChem 33032
44272391
88747398
33032
44272391
88747398
22247451
962
22247451
962
5893
5893
5886
5886
51
51
222
222
1038
1038
439153
439153
5884
5884
1ch6A03 Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1ch6B03 Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1ch6C03 Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1ch6D03 Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1ch6E03 Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1ch6F03 Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1hwxA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1hwxB01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1hwxC01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1hwxD01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1hwxE01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1hwxF01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1hwyA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1hwyB01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1hwyC01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1hwyD01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1hwyE01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1hwyF01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1hwzA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1hwzB01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1hwzC01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1hwzD01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1hwzE01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1hwzF01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1ch6A01 Bound:GLU Unbound Unbound Unbound Unbound Unbound Unbound
1ch6B01 Bound:GLU Unbound Unbound Unbound Unbound Unbound Unbound
1ch6C01 Bound:GLU Unbound Unbound Unbound Unbound Unbound Unbound
1ch6D01 Bound:GLU Unbound Unbound Unbound Unbound Unbound Unbound
1ch6E01 Bound:GLU Unbound Unbound Unbound Unbound Unbound Unbound
1ch6F01 Bound:GLU Unbound Unbound Unbound Unbound Unbound Unbound
1hwxA02 Bound:GLU Unbound Unbound Unbound Unbound Unbound Unbound
1hwxB02 Bound:GLU Unbound Unbound Unbound Unbound Unbound Unbound
1hwxC02 Bound:GLU Unbound Unbound Unbound Unbound Unbound Unbound
1hwxD02 Bound:GLU Unbound Unbound Unbound Unbound Unbound Unbound
1hwxE02 Bound:GLU Unbound Unbound Unbound Unbound Unbound Unbound
1hwxF02 Bound:GLU Unbound Unbound Unbound Unbound Unbound Unbound
1hwyA02 Unbound Unbound Unbound Bound:AKG Unbound Unbound Unbound
1hwyB02 Unbound Unbound Unbound Bound:AKG Unbound Unbound Unbound
1hwyC02 Unbound Unbound Unbound Bound:AKG Unbound Unbound Unbound
1hwyD02 Unbound Unbound Unbound Bound:AKG Unbound Unbound Unbound
1hwyE02 Unbound Unbound Unbound Bound:AKG Unbound Unbound Unbound
1hwyF02 Unbound Unbound Unbound Bound:AKG Unbound Unbound Unbound
1hwzA02 Bound:GLU Unbound Unbound Unbound Unbound Unbound Unbound
1hwzB02 Bound:GLU Unbound Unbound Unbound Unbound Unbound Unbound
1hwzC02 Bound:GLU Unbound Unbound Unbound Unbound Unbound Unbound
1hwzD02 Bound:GLU Unbound Unbound Unbound Unbound Unbound Unbound
1hwzE02 Bound:GLU Unbound Unbound Unbound Unbound Unbound Unbound
1hwzF02 Bound:GLU Unbound Unbound Unbound Unbound Unbound Unbound
1ch6A02 Unbound Bound:NAD_551 Unbound Unbound Unbound Unbound Unbound
1ch6B02 Unbound Bound:NAD_561 Unbound Unbound Unbound Unbound Unbound
1ch6C02 Unbound Bound:NAD_571 Unbound Unbound Unbound Unbound Unbound
1ch6D02 Unbound Bound:NAD_581 Unbound Unbound Unbound Unbound Unbound
1ch6E02 Unbound Bound:NAD_591 Unbound Unbound Unbound Unbound Unbound
1ch6F02 Unbound Bound:NAD_601 Unbound Unbound Unbound Unbound Unbound
1hwxA03 Unbound Unbound Unbound Unbound Unbound Bound:NAI_17 Unbound
1hwxB03 Unbound Unbound Unbound Unbound Unbound Bound:NAI_14 Unbound
1hwxC03 Unbound Unbound Unbound Unbound Unbound Bound:NAI_20 Unbound
1hwxD03 Unbound Unbound Unbound Unbound Unbound Bound:NAI_19 Unbound
1hwxE03 Unbound Unbound Unbound Unbound Unbound Bound:NAI_15 Unbound
1hwxF03 Unbound Unbound Unbound Unbound Unbound Bound:NAI_21 Unbound
1hwyA03 Unbound Bound:NAD_38 Unbound Unbound Unbound Unbound Unbound
1hwyB03 Unbound Bound:NAD_40 Unbound Unbound Unbound Unbound Unbound
1hwyC03 Unbound Bound:NAD_37 Unbound Unbound Unbound Unbound Unbound
1hwyD03 Unbound Bound:NAD_41 Unbound Unbound Unbound Unbound Unbound
1hwyE03 Unbound Bound:NAD_42 Unbound Unbound Unbound Unbound Unbound
1hwyF03 Unbound Bound:NAD_33 Unbound Unbound Unbound Unbound Unbound
1hwzA03 Unbound Unbound Unbound Unbound Unbound Unbound Bound:NDP
1hwzB03 Unbound Unbound Unbound Unbound Unbound Unbound Bound:NDP
1hwzC03 Unbound Unbound Unbound Unbound Unbound Unbound Bound:NDP
1hwzD03 Unbound Unbound Unbound Unbound Unbound Unbound Bound:NDP
1hwzE03 Unbound Unbound Unbound Unbound Unbound Unbound Bound:NDP
1hwzF03 Unbound Unbound Unbound Unbound Unbound Unbound Bound:NDP

Reference for Active-site residues
resource references E.C.
Swiss-prot;P00366

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1ch6A03
1ch6B03
1ch6C03
1ch6D03
1ch6E03
1ch6F03
1hwxA01
1hwxB01
1hwxC01
1hwxD01
1hwxE01
1hwxF01
1hwyA01
1hwyB01
1hwyC01
1hwyD01
1hwyE01
1hwyF01
1hwzA01
1hwzB01
1hwzC01
1hwzD01
1hwzE01
1hwzF01
1ch6A01 LYS 126
1ch6B01 LYS 126
1ch6C01 LYS 126
1ch6D01 LYS 126
1ch6E01 LYS 126
1ch6F01 LYS 126
1hwxA02 LYS 126
1hwxB02 LYS 126
1hwxC02 LYS 126
1hwxD02 LYS 126
1hwxE02 LYS 126
1hwxF02 LYS 126
1hwyA02 LYS 126
1hwyB02 LYS 126
1hwyC02 LYS 126
1hwyD02 LYS 126
1hwyE02 LYS 126
1hwyF02 LYS 126
1hwzA02 LYS 126
1hwzB02 LYS 126
1hwzC02 LYS 126
1hwzD02 LYS 126
1hwzE02 LYS 126
1hwzF02 LYS 126
1ch6A02
1ch6B02
1ch6C02
1ch6D02
1ch6E02
1ch6F02
1hwxA03
1hwxB03
1hwxC03
1hwxD03
1hwxE03
1hwxF03
1hwyA03
1hwyB03
1hwyC03
1hwyD03
1hwyE03
1hwyF03
1hwzA03
1hwzB03
1hwzC03
1hwzD03
1hwzE03
1hwzF03

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[2]
Fig.4, p.884 3
[4]
p.2749-2751
[19]
p.714

References
[1]
Resource
Comments CHARACTERIZATION.
Medline ID 74252258
PubMed ID 4365183
Journal Eur J Biochem
Year 1974
Volume 43
Pages 319-25
Authors Witzemann V, Koberstein R, Sund H, Rasched I, Jornvall H, Noack K
Title Studies of glutamate dehydrogenase: chemical modification and quantitative determination of tryptophan residues.
Related PDB
Related UniProtKB P00366
[2]
Resource
Comments
Medline ID
PubMed ID 7024012
Journal Int J Biochem
Year 1981
Volume 13
Pages 879-86
Authors Gore MG
Title L-Glutamic acid dehydrogenase.
Related PDB
Related UniProtKB
[3]
Resource
Comments
Medline ID
PubMed ID 6696727
Journal Biochem J
Year 1984
Volume 217
Pages 327-30
Authors Bell ET, Bell JE
Title Catalytic activity of bovine glutamate dehydrogenase requires a hexamer structure.
Related PDB
Related UniProtKB
[4]
Resource
Comments
Medline ID
PubMed ID 6144102
Journal Proc Natl Acad Sci U S A
Year 1984
Volume 81
Pages 2747-51
Authors Fisher HF, Viswanathan TS
Title Carbonyl oxygen exchange evidence of imine formation in the glutamate dehydrogenase reaction and identification of the "occult role" of NADPH.
Related PDB
Related UniProtKB
[5]
Resource
Comments
Medline ID
PubMed ID 3442667
Journal Biochemistry
Year 1987
Volume 26
Pages 8443-50
Authors Banerjee A, Levy HR, Levy GC, LiMuti C, Goldstein BM, Bell JE
Title A transfer nuclear Overhauser effect study of coenzyme binding to distinct sites in binary and ternary complexes in glutamate dehydrogenase.
Related PDB
Related UniProtKB
[6]
Resource
Comments
Medline ID
PubMed ID 3569640
Journal Int J Biochem
Year 1987
Volume 19
Pages 53-61
Authors Pour-Rahimi F, Nemat-Gorgani M
Title Reversible association of ox liver glutamate dehydrogenase with the inner mitochondrial membrane.
Related PDB
Related UniProtKB
[7]
Resource
Comments
Medline ID
PubMed ID 3149742
Journal Protein Eng
Year 1988
Volume 2
Pages 147-52
Authors McPherson MJ, Baron AJ, Jones KM, Price GJ, Wootton JC
Title Multiple interactions of lysine-128 of Escherichia coli glutamate dehydrogenase revealed by site-directed mutagenesis studies.
Related PDB
Related UniProtKB
[8]
Resource
Comments
Medline ID
PubMed ID 2575093
Journal J Biochem (Tokyo)
Year 1989
Volume 106
Pages 515-7
Authors Nakajima N, Nakamura K, Esaki N, Tanaka H, Soda K
Title Enzymatic in situ analysis by 1H-NMR of the hydrogen transfer stereospecificity of NAD(P)+-dependent dehydrogenases.
Related PDB
Related UniProtKB
[9]
Resource
Comments
Medline ID
PubMed ID 1743279
Journal FEBS Lett
Year 1991
Volume 294
Pages 1-5
Authors Fisher HF, Singh N
Title Transduction of enzyme-ligand binding energy into catalytic driving force.
Related PDB
Related UniProtKB
[10]
Resource
Comments
Medline ID
PubMed ID 7961946
Journal J Biol Chem
Year 1994
Volume 269
Pages 29592-7
Authors Saha SK, Maniscalco SJ, Singh N, Fisher HF
Title The demonstration of a glutamate dehydrogenase-NADP-L-glutamate charge-transfer complex and its location on the reaction pathway.
Related PDB
Related UniProtKB
[11]
Resource
Comments
Medline ID
PubMed ID 9356294
Journal J Struct Biol
Year 1997
Volume 120
Pages 73-7
Authors Peterson PE, Pierce J, Smith TJ
Title Crystallization and characterization of bovine liver glutamate dehydrogenase.
Related PDB
Related UniProtKB
[12]
Resource
Comments
Medline ID
PubMed ID 9772187
Journal Biochemistry
Year 1998
Volume 37
Pages 14585-90
Authors Maniscalco SJ, Saha SK, Fisher HF
Title Identification and characterization of kinetically competent carbinolamine and alpha-iminoglutarate complexes in the glutamate dehydrogenase-catalyzed oxidation of L-glutamate using a multiwavelength transient state approach.
Related PDB
Related UniProtKB
[13]
Resource
Comments
Medline ID
PubMed ID 10318805
Journal J Biol Chem
Year 1999
Volume 274
Pages 13948-53
Authors Cho SW, Yoon HY
Title Photoaffinity labeling of brain glutamate dehydrogenase isoproteins with an azido-ADP.
Related PDB
Related UniProtKB
[14]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
Medline ID 99354411
PubMed ID 10425679
Journal Structure Fold Des
Year 1999
Volume 7
Pages 769-82
Authors Peterson PE, Smith TJ
Title The structure of bovine glutamate dehydrogenase provides insights into the mechanism of allostery.
Related PDB 1ch6 1hwx
Related UniProtKB P00366
[15]
Resource
Comments
Medline ID
PubMed ID 11554732
Journal Biochem Biophys Res Commun
Year 2001
Volume 287
Pages 343-7
Authors Fisher HF, Maniscalco SJ, Tally J
Title Stabilization of noncovalent intermediates in enzymatically catalyzed reactions.
Related PDB
Related UniProtKB
[16]
Resource
Comments
Medline ID
PubMed ID 11327816
Journal Biochemistry
Year 2001
Volume 40
Pages 1577-86
Authors Madhusoodanan KS, Colman RF
Title Adenosine 5'-0-[S-(4-succinimidyl-benzophenone)thiophosphate]: a new photoaffinity label of the allosteric ADP site of bovine liver glutamate dehydrogenase.
Related PDB
Related UniProtKB
[17]
Resource
Comments
Medline ID
PubMed ID 11389722
Journal Eur J Biochem
Year 2001
Volume 268
Pages 3205-13
Authors Cho SW, Yoon HY, Ahn JY, Lee EY, Lee J
Title Cassette mutagenesis of lysine 130 of human glutamate dehydrogenase. An essential residue in catalysis.
Related PDB
Related UniProtKB
[18]
Resource
Comments
Medline ID
PubMed ID 11686930
Journal J Biochem (Tokyo)
Year 2001
Volume 130
Pages 671-7
Authors Ghobadi S, Safarian S, Moosavi-Movahedi AA, Ranjbar B
Title Octyl glucoside induced formation of the molten globule-like state of glutamate dehydrogenase.
Related PDB
Related UniProtKB
[19]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 11254391
Journal J Mol Biol
Year 2001
Volume 307
Pages 707-20
Authors Smith TJ, Peterson PE, Schmidt T, Fang J, Stanley CA
Title Structures of bovine glutamate dehydrogenase complexes elucidate the mechanism of purine regulation.
Related PDB 1hwy 1hwz
Related UniProtKB
[20]
Resource
Comments
Medline ID
PubMed ID 12324473
Journal J Biol Chem
Year 2002
Volume 277
Pages 46552-8
Authors Zaganas I, Spanaki C, Karpusas M, Plaitakis A
Title Substitution of Ser for Arg-443 in the regulatory domain of human housekeeping (GLUD1) glutamate dehydrogenase virtually abolishes basal activity and markedly alters the activation of the enzyme by ADP and L-leucine.
Related PDB
Related UniProtKB
[21]
Resource
Comments
Medline ID
PubMed ID 11950837
Journal J Biol Chem
Year 2002
Volume 277
Pages 26422-8
Authors Zaganas I, Plaitakis A
Title Single amino acid substitution (G456A) in the vicinity of the GTP binding domain of human housekeeping glutamate dehydrogenase markedly attenuates GTP inhibition and abolishes the cooperative behavior of the enzyme.
Related PDB
Related UniProtKB
[22]
Resource
Comments
Medline ID
PubMed ID 12054821
Journal J Mol Biol
Year 2002
Volume 318
Pages 765-77
Authors Smith TJ, Schmidt T, Fang J, Wu J, Siuzdak G, Stanley CA
Title The structure of apo human glutamate dehydrogenase details subunit communication and allostery.
Related PDB 1l1f
Related UniProtKB

Comments
This enzyme has got a second coenzyme subsite for NAD(P), which seems to be involved in regulation.

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