L-phenylalanine dehydrogenase

Name	L-phenylalanine dehydrogenase
Synonyms	1.4.1.20 PheDH
Gene Name	pdh
Organism	Rhodococcus sp.
Amino acid sequence	>lcl\|BSEQ0012865\|Phenylalanine dehydrogenase MSIDSALNWDGEMTVTRFDRETGAHFVIRLDSTQLGPAAGGTRAAQYSQLADALTDAGKL AGAMTLKMAVSNLPMGGGKSVIALPAPRHSIDPSTWARILRIHAENIDKLSGNYWTGPDV NTNSADMDTLNDTTEFVFGRSLERGGAGSSAFTTAVGVFEAMKATVAHRGLGSLDGLTVL VQGLGAVGGSLASLAAEAGAQLLVADTDTERVAHAVALGHTAVALEDVLSTPCDVFAPCA MGGVITTEVARTLDCSVVAGAANNVIADEAASDILHARGILYAPDFVANAGGAIHLVGRE VLGWSESVVHERAVAIGDTLNQVFEISDNDGVTPDEAARTLAGRRAREASTTTATA
Number of residues	None
Molecular Weight	36608.615
Theoretical pI	4.55
GO Classification	Functions nucleotide binding phenylalanine dehydrogenase activity Processes L-phenylalanine catabolic process L-phenylalanine biosynthetic process Components
General Function	Phenylalanine dehydrogenase activity
Specific Function	Catalyzes the reversible, NAD-dependent deamination of L-phenylalanine to phenyl pyruvate, ammonia and NADH.
Transmembrane Regions
GenBank Protein ID
UniProtKB ID	Q59771
UniProtKB Entry Name
Cellular Location	None
Gene sequence	>lcl\|BSEQ0007840\|1071 bp ATGAGTATCGACAGCGCACTGAACTGGGACGGGGAAATGACGGTCACCCGATTCGACCGG GAGACTGGTGCCCATTTCGTCATTCGACTCGATTCGACCCAACTCGGACCGGCGGCCGGA GGCACCAGAGCCGCACAGTACTCACAGCTGGCGGACGCCCTCACCGACGCCGGCAAATTG GCGGGGGCGATGACGTTGAAGATGGCAGTGAGCAACCTTCCGATGGGCGGGGGCAAATCC GTCATTGCGCTTCCTGCGCCGCGTCATTCGATCGATCCGAGCACGTGGGCACGCATCCTC CGAATCCACGCCGAGAACATCGACAAGTTGTCCGGCAACTACTGGACCGGACCGGACGTC AACACCAATTCGGCAGACATGGATACTCTGAACGACACCACCGAGTTCGTGTTCGGACGG TCGCTCGAACGCGGCGGCGCGGGTTCGAGCGCGTTCACCACCGCCGTTGGCGTGTTCGAG GCGATGAAGGCGACCGTCGCGCACCGTGGGCTGGGCTCACTCGACGGTTTGACGGTCCTG GTCCAAGGACTGGGGGCAGTCGGAGGATCATTGGCATCCCTGGCCGCCGAAGCGGGTGCG CAACTCCTGGTGGCAGACACCGACACCGAGCGAGTAGCGCACGCTGTTGCGTTGGGCCAC ACAGCGGTTGCCCTCGAGGACGTTCTGTCCACCCCGTGTGATGTCTTCGCACCCTGCGCA ATGGGCGGCGTCATCACCACCGAGGTGGCGCGAACACTCGACTGTTCCGTCGTGGCCGGT GCCGCCAACAACGTCATCGCCGACGAGGCCGCCTCGGACATCCTGCACGCACGCGGAATT CTGTACGCTCCCGACTTCGTGGCCAACGCCGGCGGTGCCATCCACCTCGTAGGCCGGGAG GTTCTCGGTTGGTCCGAGTCGGTTGTCCACGAACGAGCAGTTGCCATAGGCGACACCCTG AATCAGGTCTTCGAGATCTCCGACAACGACGGCGTCACCCCGGACGAGGCCGCCCGCACT CTCGCTGGACGGCGCGCCCGCGAGGCCTCGACAACGACAGCGACTGCCTAG
GenBank Gene ID
GeneCard ID	None
GenAtlas ID
HGNC ID
Chromosome Location	None
Locus	None
References	Brunhuber NM, Banerjee A, Jacobs WR Jr, Blanchard JS: Cloning, sequencing, and expression of Rhodococcus L-phenylalanine dehydrogenase. Sequence comparisons to amino-acid dehydrogenases. J Biol Chem. 1994 Jun 10;269(23):16203-11. [8206922 ] Vanhooke JL, Thoden JB, Brunhuber NM, Blanchard JS, Holden HM: Phenylalanine dehydrogenase from Rhodococcus sp. M4: high-resolution X-ray analyses of inhibitory ternary complexes reveal key features in the oxidative deamination mechanism. Biochemistry. 1999 Feb 23;38(8):2326-39. [10029526 ] Brunhuber NM, Thoden JB, Blanchard JS, Vanhooke JL: Rhodococcus L-phenylalanine dehydrogenase: kinetics, mechanism, and structural basis for catalytic specificity. Biochemistry. 2000 Aug 8;39(31):9174-87. [10924111 ]

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