EzCatDB: D00035
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DB codeD00035
CATH domainDomain 13.40.192.10 : Leucine Dehydrogenase; Chain A, domain 1Catalytic domain
Domain 23.40.50.720 : Rossmann foldCatalytic domain
E.C.1.4.1.20

CATH domainRelated DB codes (homologues)
3.40.192.10 : Leucine Dehydrogenase; Chain A, domain 1D00458,D00032,D00033,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,D00033,D00034,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

Q59771P97014
Protein name
Phenylalanine dehydrogenasephenylalanine dehydrogenase
L-phenylalanine dehydrogenase
PHD
SynonymsL-phenylalanine dehydrogenase
EC 1.4.1.20
PheDH
EC 1.4.1.20
PfamPF00208 (ELFV_dehydrog)
PF02812 (ELFV_dehydrog_N)
[Graphical view]
PF00208 (ELFV_dehydrog)
PF02812 (ELFV_dehydrog_N)
[Graphical view]

KEGG pathways
MAP codePathways
MAP00360Phenylalanine metabolism
MAP00400Phenylalanine, tyrosine and tryptophan biosynthesis

UniProtKB:Accession NumberQ59771P97014
Entry nameQ59771_RHOSODHPH_SPOUR
Activity
L-phenylalanine + H(2)O + NAD(+) = phenylpyruvate + NH(3) + NADH.
Subunit

Subcellular location

Cofactor


Compound table: links to PDB-related databases & PoSSuM

SubstratesProducts
KEGG-idC00079C00001C00003C00166C00014C00004C00080
CompoundL-PhenylalanineH2ONAD+PhenylpyruvateNH3NADHH+
Typeamino acids,aromatic ring (only carbon atom)H2Oamide group,amine group,nucleotidearomatic ring (only carbon atom),carbohydrate,carboxyl groupamine group,organic ionamide group,amine group,nucleotideothers
ChEBI17295
58095
15377
15846
30851
16134
16908
15378
PubChem6925665
6140
962
22247451
5893
997
222
439153
1038
               
1bw9A01Unbound UnboundBound:PPYUnboundUnbound 
1bw9B01Unbound UnboundBound:PPYUnboundUnbound 
1bxgA01Analogue:HCI UnboundUnboundUnboundUnbound 
1bxgB01Analogue:HCI UnboundUnboundUnboundUnbound 
1bw9A02Unbound Bound:NADUnboundUnboundUnbound 
1bw9B02Unbound Analogue:NADUnboundUnboundUnbound 
1bxgA02Unbound Bound:NADUnboundUnboundUnbound 
1bxgB02Unbound Bound:NADUnboundUnboundUnbound 

Active-site residues
resource
Swiss-prot & literature [3]
pdbCatalytic residues
         
1bw9A01LYS  78;ASP 118
1bw9B01LYS 478;ASP 518
1bxgA01LYS  78;ASP 118
1bxgB01LYS 478;ASP 518
1bw9A02 
1bw9B02 
1bxgA02 
1bxgB02 

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[3]p.2336-2338, Fig.88
[4]Fig.75

references
[1]same as D00033-5
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.
[2]
PubMed ID9761891
JournalActa Crystallogr D Biol Crystallogr
Year1998
Volume54
Pages269-72
AuthorsPasquo A, Britton KL, Baker PJ, Brearley G, Hinton RJ, Moir AJ, Stillman TJ, Rice DW
TitleCrystallization of NAD+-dependent phenylalanine dehydrogenase from Nocardia sp239.
[3]
CommentsX-ray crystallography
PubMed ID10029526
JournalBiochemistry
Year1999
Volume38
Pages2326-39
AuthorsVanhooke JL, Thoden JB, Brunhuber NM, Blanchard JS, Holden HM
TitlePhenylalanine dehydrogenase from Rhodococcus sp. M4: high-resolution X-ray analyses of inhibitory ternary complexes reveal key features in the oxidative deamination mechanism.
Related PDB1bw9,1bxg
[4]
PubMed ID10924111
JournalBiochemistry
Year2000
Volume39
Pages9174-87
AuthorsBrunhuber NM, Thoden JB, Blanchard JS, Vanhooke JL
TitleRhodococcus L-phenylalanine dehydrogenase: kinetics, mechanism, and structural basis for catalytic specificity.


createdupdated
2004-03-172009-03-30


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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)
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