DB code: D00033

CATH domain 3.40.192.10 : Leucine Dehydrogenase; Chain A, domain 1 Catalytic domain
3.40.50.720 : Rossmann fold
E.C. 1.4.1.9
CSA
M-CSA
MACiE

CATH domain Related DB codes (homologues)
3.40.192.10 : Leucine Dehydrogenase; Chain A, domain 1 D00458 D00032 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 D00032 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 Pfam
P13154 Leucine dehydrogenase
LeuDH
EC 1.4.1.9
PF00208 (ELFV_dehydrog)
PF02812 (ELFV_dehydrog_N)
[Graphical View]
Q7SIB4
Oxidoreductase
PF00208 (ELFV_dehydrog)
PF02812 (ELFV_dehydrog_N)
[Graphical View]

KEGG enzyme name
leucine dehydrogenase
L-leucine dehydrogenase
L-leucine:NAD+ oxidoreductase, deaminating
LeuDH

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P13154 DHLE_BACST L-leucine + H(2)O + NAD(+) = 4-methyl-2- oxopentanoate + NH(3) + NADH. Homohexamer.
Q7SIB4 Q7SIB4_BACSH

KEGG Pathways
Map code Pathways E.C.
MAP00280 Valine, leucine and isoleucine degradation
MAP00290 Valine, leucine and isoleucine biosynthesis

Compound table
Substrates Products Intermediates
KEGG-id C00123 C00001 C00003 C00233 C00014 C00004 C00080
E.C.
Compound L-Leucine H2O NAD+ 4-Methyl-2-oxopentanoate NH3 NADH H+
Type amino acids H2O amide group,amine group,nucleotide carbohydrate,carboxyl group amine group,organic ion amide group,amine group,nucleotide others
ChEBI 15603
 57427
 15603
 57427
 		15377
 15377
 		15846
 15846
 		48430
 48430
 		16134
 16134
 		16908
 16908
 		15378
 15378
PubChem 6106
 7045798
 6106
 7045798
 		22247451
 962
 22247451
 962
 		5893
 5893
 		70
 70
 		222
 222
 		439153
 439153
 		1038
 1038
1lehA01 Unbound Unbound Unbound Unbound Unbound
1lehB01 Unbound Unbound Unbound Unbound Unbound
1lehA02 Unbound Unbound Unbound Unbound Unbound
1lehB02 Unbound Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
Swiss-prot;P13154, literature [7]

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1lehA01 LYS 80;ASP 115
1lehB01 LYS 80;ASP 115
1lehA02
1lehB02

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[2]
Fig. 4, p.27045
[3]
p.942
[7]
p.701
[9]
p.25109

References
[1]
Resource
Comments ACTIVE SITE LYS-80
Medline ID 93015789
PubMed ID 1400267
Journal J Biochem (Tokyo)
Year 1992
Volume 112
Pages 258-65
Authors Matsuyama T, Soda K, Fukui T, Tanizawa K
Title Leucine dehydrogenase from Bacillus stearothermophilus: identification of active-site lysine by modification with pyridoxal phosphate.
Related PDB
Related UniProtKB P13154
[2]
Resource
Comments
Medline ID
PubMed ID 8262941
Journal J Biol Chem
Year 1993
Volume 268
Pages 27039-45
Authors Sekimoto T, Matsuyama T, Fukui T, Tanizawa K
Title Evidence for lysine 80 as general base catalyst of leucine dehydrogenase.
Related PDB
Related UniProtKB
[3]
Resource
Comments
Medline ID
PubMed ID 8263939
Journal J Mol Biol
Year 1993
Volume 234
Pages 938-45
Authors Britton KL, Baker PJ, Engel PC, Rice DW, Stillman TJ
Title Evolution of substrate diversity in the superfamily of amino acid dehydrogenases. Prospects for rational chiral synthesis.
Related PDB
Related UniProtKB
[4]
Resource
Comments
Medline ID
PubMed ID 7798175
Journal J Biochem (Tokyo)
Year 1994
Volume 116
Pages 176-82
Authors Sekimoto T, Fukui T, Tanizawa K
Title Role of the conserved glycyl residues located at the active site of leucine dehydrogenase from Bacillus stearothermophilus.
Related PDB
Related UniProtKB
[5]
Resource
Comments
Medline ID
PubMed ID 7883771
Journal J Biochem (Tokyo)
Year 1994
Volume 116
Pages 931-6
Authors Kataoka K, Takada H, Tanizawa K, Yoshimura T, Esaki N, Ohshima T, Soda K
Title Construction and characterization of chimeric enzyme consisting of an amino-terminal domain of phenylalanine dehydrogenase and a carboxy-terminal domain of leucine dehydrogenase.
Related PDB
Related UniProtKB
[6]
Resource
Comments
Medline ID
PubMed ID 8107149
Journal J Mol Biol
Year 1994
Volume 236
Pages 663-5
Authors Turnbull AP, Ashford SR, Baker PJ, Rice DW, Rodgers FH, Stillman TJ, Hanson RL
Title Crystallization and quaternary structure analysis of the NAD(+)-dependent leucine dehydrogenase from Bacillus sphaericus.
Related PDB
Related UniProtKB
[7]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
Medline ID
PubMed ID 8591046
Journal Structure
Year 1995
Volume 3
Pages 693-705
Authors Baker PJ, Turnbull AP, Sedelnikova SE, Stillman TJ, Rice DW
Title A role for quaternary structure in the substrate specificity of leucine dehydrogenase.
Related PDB 1leh
Related UniProtKB Q7SIB4
[8]
Resource
Comments
Medline ID
PubMed ID 9405044
Journal Biochemistry
Year 1997
Volume 36
Pages 16109-15
Authors Baker PJ, Waugh ML, Wang XG, Stillman TJ, Turnbull AP, Engel PC, Rice DW
Title Determinants of substrate specificity in the superfamily of amino acid dehydrogenases.
Related PDB
Related UniProtKB
[9]
Resource
Comments
Medline ID
PubMed ID 9312120
Journal J Biol Chem
Year 1997
Volume 272
Pages 25105-11
Authors Turnbull AP, Baker PJ, Rice DW
Title Analysis of the quaternary structure, substrate specificity, and catalytic mechanism of valine dehydrogenase.
Related PDB
Related UniProtKB
[10]
Resource
Comments
Medline ID
PubMed ID 11162651
Journal Biochem Biophys Res Commun
Year 2001
Volume 280
Pages 1177-82
Authors Oikawa T, Kataoka K, Jin Y, Suzuki S, Soda K
Title Fragmentary form of thermostable leucine dehydrogenase of Bacillus stearothermophilus: its construction and reconstitution of active fragmentary enzyme.
Related PDB
Related UniProtKB

Comments
Accoriding to the catalytic mechanism proposed in the literature [2], this enzyme catalyzes the following reactions:
(A) Hydride transfer from C-alpha (of Leu) to nicotinamide ring (of NAD)
(B) Schiff-base deformation

Created Updated
2005-02-08 2009-02-26