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)
3.40.50.720 : 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
3.40.192.10 : Leucine Dehydrogenase; Chain A, domain 1 D00458 D00032 D00033 D00605 D00845 D00857 D00858 M00210 T00010 T00011 T00414

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
P97014 DHPH_SPOUR L-phenylalanine + H(2)O + NAD(+) = phenylpyruvate + NH(3) + NADH.
Q59771 Q59771_RHOSO

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

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
15377
15846
30851
16134
16908
15378
PubChem 6140
6925665
22247451
962
5893
997
222
439153
1038
1bw9A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Bound:PPY Unbound Unbound
1bw9B01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Bound:PPY Unbound Unbound
1bxgA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Analogue:HCI Unbound Unbound Unbound Unbound
1bxgB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Analogue:HCI Unbound Unbound Unbound Unbound
1bw9A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Bound:NAD Unbound Unbound Unbound
1bw9B02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Analogue:NAD Unbound Unbound Unbound
1bxgA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Bound:NAD Unbound Unbound Unbound
1bxgB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain 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 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain LYS 78;ASP 118
1bw9B01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain LYS 478;ASP 518
1bxgA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain LYS 78;ASP 118
1bxgB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain LYS 478;ASP 518
1bw9A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1bw9B02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1bxgA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1bxgB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain

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