EzCatDB: D00033
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DB codeD00033
CATH domainDomain 13.40.192.10 : Leucine Dehydrogenase; Chain A, domain 1Catalytic domain
Domain 23.40.50.720 : Rossmann fold
E.C.1.4.1.9

CATH domainRelated DB codes (homologues)
3.40.192.10 : Leucine Dehydrogenase; Chain A, domain 1D00458,D00032,D00035,D00605,D00845,D00857,D00858,M00210,T00010,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,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

Enzyme Name
UniProtKBKEGG

P13154Q7SIB4
Protein nameLeucine dehydrogenase
leucine dehydrogenase
L-leucine dehydrogenase
L-leucine:NAD+ oxidoreductase, deaminating
LeuDH
SynonymsLeuDH
EC 1.4.1.9
Oxidoreductase
PfamPF00208 (ELFV_dehydrog)
PF02812 (ELFV_dehydrog_N)
[Graphical view]
PF00208 (ELFV_dehydrog)
PF02812 (ELFV_dehydrog_N)
[Graphical view]

KEGG pathways
MAP codePathways
MAP00280Valine, leucine and isoleucine degradation
MAP00290Valine, leucine and isoleucine biosynthesis

UniProtKB:Accession NumberP13154Q7SIB4
Entry nameDHLE_BACSTQ7SIB4_BACSH
ActivityL-leucine + H(2)O + NAD(+) = 4-methyl-2- oxopentanoate + NH(3) + NADH.
SubunitHomohexamer.
Subcellular location

Cofactor


Compound table: links to PDB-related databases & PoSSuM

SubstratesProducts
KEGG-idC00123C00001C00003C00233C00014C00004C00080
CompoundL-LeucineH2ONAD+4-Methyl-2-oxopentanoateNH3NADHH+
Typeamino acidsH2Oamide group,amine group,nucleotidecarbohydrate,carboxyl groupamine group,organic ionamide group,amine group,nucleotideothers
ChEBI15603
57427
15377
15846
48430
16134
16908
15378
PubChem7045798
6106
962
22247451
5893
70
222
439153
1038
               
1lehA01Unbound UnboundUnboundUnboundUnbound 
1lehB01Unbound UnboundUnboundUnboundUnbound 
1lehA02Unbound UnboundUnboundUnboundUnbound 
1lehB02Unbound UnboundUnboundUnboundUnbound 

Active-site residues
resource
Swiss-prot;P13154, literature [7]
pdbCatalytic residues
         
1lehA01LYS 80;ASP 115
1lehB01LYS 80;ASP 115
1lehA02 
1lehB02 

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[2]Fig. 4, p.27045
[3]p.942
[7]p.701
[9]p.25109

references
[1]
CommentsACTIVE SITE LYS-80
Medline ID93015789
PubMed ID1400267
JournalJ Biochem (Tokyo)
Year1992
Volume112
Pages258-65
AuthorsMatsuyama T, Soda K, Fukui T, Tanizawa K
TitleLeucine dehydrogenase from Bacillus stearothermophilus: identification of active-site lysine by modification with pyridoxal phosphate.
Related UniProtKBP13154
[2]
PubMed ID8262941
JournalJ Biol Chem
Year1993
Volume268
Pages27039-45
AuthorsSekimoto T, Matsuyama T, Fukui T, Tanizawa K
TitleEvidence for lysine 80 as general base catalyst of leucine dehydrogenase.
[3]
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.
[4]
PubMed ID7798175
JournalJ Biochem (Tokyo)
Year1994
Volume116
Pages176-82
AuthorsSekimoto T, Fukui T, Tanizawa K
TitleRole of the conserved glycyl residues located at the active site of leucine dehydrogenase from Bacillus stearothermophilus.
[5]
PubMed ID7883771
JournalJ Biochem (Tokyo)
Year1994
Volume116
Pages931-6
AuthorsKataoka K, Takada H, Tanizawa K, Yoshimura T, Esaki N, Ohshima T, Soda K
TitleConstruction and characterization of chimeric enzyme consisting of an amino-terminal domain of phenylalanine dehydrogenase and a carboxy-terminal domain of leucine dehydrogenase.
[6]
PubMed ID8107149
JournalJ Mol Biol
Year1994
Volume236
Pages663-5
AuthorsTurnbull AP, Ashford SR, Baker PJ, Rice DW, Rodgers FH, Stillman TJ, Hanson RL
TitleCrystallization and quaternary structure analysis of the NAD(+)-dependent leucine dehydrogenase from Bacillus sphaericus.
[7]
CommentsX-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
PubMed ID8591046
JournalStructure
Year1995
Volume3
Pages693-705
AuthorsBaker PJ, Turnbull AP, Sedelnikova SE, Stillman TJ, Rice DW
TitleA role for quaternary structure in the substrate specificity of leucine dehydrogenase.
Related PDB1leh
Related UniProtKBQ7SIB4
[8]
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.
[9]
PubMed ID9312120
JournalJ Biol Chem
Year1997
Volume272
Pages25105-11
AuthorsTurnbull AP, Baker PJ, Rice DW
TitleAnalysis of the quaternary structure, substrate specificity, and catalytic mechanism of valine dehydrogenase.
[10]
PubMed ID11162651
JournalBiochem Biophys Res Commun
Year2001
Volume280
Pages1177-82
AuthorsOikawa T, Kataoka K, Jin Y, Suzuki S, Soda K
TitleFragmentary form of thermostable leucine dehydrogenase of Bacillus stearothermophilus: its construction and reconstitution of active fragmentary enzyme.

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

createdupdated
2005-02-082009-02-26


Copyright: Nozomi Nagano, JST & CBRC-AIST
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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) (September 2005 - September 2008)
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)
Supported by the commission for the Development of Artificial Gene Synthesis Technology for Creating Innovative Biomaterial from the Ministry of Economy, Trade and Industry (METI) (October 2012 - )
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