Phenylalanine dehydrogenase
Details
- Name
- 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
- 356
- Molecular Weight
- 36608.615
- Theoretical pI
- 4.55
- GO Classification
- Functionsnucleotide binding / phenylalanine dehydrogenase activityProcessesL-phenylalanine biosynthetic process / L-phenylalanine catabolic process
- General Function
- Phenylalanine dehydrogenase activity
- Specific Function
- Catalyzes the reversible, NAD-dependent deamination of L-phenylalanine to phenyl pyruvate, ammonia and NADH.
- Pfam Domain Function
- Transmembrane Regions
- Not Available
- Cellular Location
- Not Available
- Gene sequence
>lcl|BSEQ0007840|1071 bp ATGAGTATCGACAGCGCACTGAACTGGGACGGGGAAATGACGGTCACCCGATTCGACCGG GAGACTGGTGCCCATTTCGTCATTCGACTCGATTCGACCCAACTCGGACCGGCGGCCGGA GGCACCAGAGCCGCACAGTACTCACAGCTGGCGGACGCCCTCACCGACGCCGGCAAATTG GCGGGGGCGATGACGTTGAAGATGGCAGTGAGCAACCTTCCGATGGGCGGGGGCAAATCC GTCATTGCGCTTCCTGCGCCGCGTCATTCGATCGATCCGAGCACGTGGGCACGCATCCTC CGAATCCACGCCGAGAACATCGACAAGTTGTCCGGCAACTACTGGACCGGACCGGACGTC AACACCAATTCGGCAGACATGGATACTCTGAACGACACCACCGAGTTCGTGTTCGGACGG TCGCTCGAACGCGGCGGCGCGGGTTCGAGCGCGTTCACCACCGCCGTTGGCGTGTTCGAG GCGATGAAGGCGACCGTCGCGCACCGTGGGCTGGGCTCACTCGACGGTTTGACGGTCCTG GTCCAAGGACTGGGGGCAGTCGGAGGATCATTGGCATCCCTGGCCGCCGAAGCGGGTGCG CAACTCCTGGTGGCAGACACCGACACCGAGCGAGTAGCGCACGCTGTTGCGTTGGGCCAC ACAGCGGTTGCCCTCGAGGACGTTCTGTCCACCCCGTGTGATGTCTTCGCACCCTGCGCA ATGGGCGGCGTCATCACCACCGAGGTGGCGCGAACACTCGACTGTTCCGTCGTGGCCGGT GCCGCCAACAACGTCATCGCCGACGAGGCCGCCTCGGACATCCTGCACGCACGCGGAATT CTGTACGCTCCCGACTTCGTGGCCAACGCCGGCGGTGCCATCCACCTCGTAGGCCGGGAG GTTCTCGGTTGGTCCGAGTCGGTTGTCCACGAACGAGCAGTTGCCATAGGCGACACCCTG AATCAGGTCTTCGAGATCTCCGACAACGACGGCGTCACCCCGGACGAGGCCGCCCGCACT CTCGCTGGACGGCGCGCCCGCGAGGCCTCGACAACGACAGCGACTGCCTAG
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID Q59771 UniProtKB Entry Name DHPH_RHOSO GenBank Protein ID 475596 GenBank Gene ID U08381 - General 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. [Article]
- 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. [Article]
- 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. [Article]