DB code: D00035

CATH domain 3.40.192.10 : Leucine Dehydrogenase; Chain A, domain 1 Catalytic domain
3.40.50.720 : Rossmann fold Catalytic domain
E.C. 1.4.1.20
CSA
M-CSA
MACiE

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

Uniprot Enzyme Name
UniprotKB Protein name Synonyms Pfam
Q59771
L-phenylalanine dehydrogenase
EC 1.4.1.20
PF00208 (ELFV_dehydrog)
PF02812 (ELFV_dehydrog_N)
[Graphical View]
P97014 Phenylalanine dehydrogenase
PheDH
EC 1.4.1.20
PF00208 (ELFV_dehydrog)
PF02812 (ELFV_dehydrog_N)
[Graphical View]

KEGG enzyme name
phenylalanine dehydrogenase
L-phenylalanine dehydrogenase
PHD

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
Q59771 Q59771_RHOSO
P97014 DHPH_SPOUR L-phenylalanine + H(2)O + NAD(+) = phenylpyruvate + NH(3) + NADH.

KEGG Pathways
Map code Pathways E.C.
MAP00360 Phenylalanine metabolism
MAP00400 Phenylalanine, tyrosine and tryptophan biosynthesis

Compound table
Substrates Products Intermediates
KEGG-id C00079 C00001 C00003 C00166 C00014 C00004 C00080
E.C.
Compound L-Phenylalanine H2O NAD+ Phenylpyruvate NH3 NADH H+
Type amino acids,aromatic ring (only carbon atom) H2O amide group,amine group,nucleotide aromatic ring (only carbon atom),carbohydrate,carboxyl group amine group,organic ion amide group,amine group,nucleotide others
ChEBI 17295
 58095
 17295
 58095
 		15377
 15377
 		15846
 15846
 		30851
 30851
 		16134
 16134
 		16908
 16908
 		15378
 15378
PubChem 6140
 6925665
 6140
 6925665
 		22247451
 962
 22247451
 962
 		5893
 5893
 		997
 997
 		222
 222
 		439153
 439153
 		1038
 1038
1bw9A01 Unbound Unbound Bound:PPY Unbound Unbound
1bw9B01 Unbound Unbound Bound:PPY Unbound Unbound
1bxgA01 Analogue:HCI Unbound Unbound Unbound Unbound
1bxgB01 Analogue:HCI Unbound Unbound Unbound Unbound
1bw9A02 Unbound Bound:NAD Unbound Unbound Unbound
1bw9B02 Unbound Analogue:NAD Unbound Unbound Unbound
1bxgA02 Unbound Bound:NAD Unbound Unbound Unbound
1bxgB02 Unbound Bound:NAD Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
Swiss-prot & literature [3]

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1bw9A01 LYS 78;ASP 118
1bw9B01 LYS 478;ASP 518
1bxgA01 LYS 78;ASP 118
1bxgB01 LYS 478;ASP 518
1bw9A02
1bw9B02
1bxgA02
1bxgB02

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[3]
p.2336-2338, Fig.8 8
[4]
Fig.7 5

References
[1]
Resource same as D00033-5
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
[2]
Resource
Comments
Medline ID
PubMed ID 9761891
Journal Acta Crystallogr D Biol Crystallogr
Year 1998
Volume 54
Pages 269-72
Authors Pasquo A, Britton KL, Baker PJ, Brearley G, Hinton RJ, Moir AJ, Stillman TJ, Rice DW
Title Crystallization of NAD+-dependent phenylalanine dehydrogenase from Nocardia sp239.
Related PDB
Related UniProtKB
[3]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 10029526
Journal Biochemistry
Year 1999
Volume 38
Pages 2326-39
Authors Vanhooke JL, Thoden JB, Brunhuber NM, Blanchard JS, Holden HM
Title Phenylalanine dehydrogenase from Rhodococcus sp. M4: high-resolution X-ray analyses of inhibitory ternary complexes reveal key features in the oxidative deamination mechanism.
Related PDB 1bw9 1bxg
Related UniProtKB
[4]
Resource
Comments
Medline ID
PubMed ID 10924111
Journal Biochemistry
Year 2000
Volume 39
Pages 9174-87
Authors Brunhuber NM, Thoden JB, Blanchard JS, Vanhooke JL
Title Rhodococcus L-phenylalanine dehydrogenase: kinetics, mechanism, and structural basis for catalytic specificity.
Related PDB
Related UniProtKB

Comments

Created Updated
2004-03-17 2009-03-30