Tyrosine phenol-lyase
Details
- Name
- Tyrosine phenol-lyase
- Synonyms
- 4.1.99.2
- Beta-tyrosinase
- Gene Name
- tpl
- Organism
- Citrobacter freundii
- Amino acid sequence
>lcl|BSEQ0012870|Tyrosine phenol-lyase MNYPAEPFRIKSVETVSMIPRDERLKKMQEAGYNTFLLNSKDIYIDLLTDSGTNAMSDKQ WAGMMMGDEAYAGSENFYHLERTVQELFGFKHIVPTHQGRGAENLLSQLAIKPGQYVAGN MYFTTTRYHQEKNGAVFVDIVRDEAHDAGLNIAFKGDIDLKKLQKLIDEKGAENIAYICL AVTVNLAGGQPVSMANMRAVRELTEAHGIKVFYDATRCVENAYFIKEQEQGFENKSIAEI VHEMFSYADGCTMSGKKDCLVNIGGFLCMNDDEMFSSAKELVVVYEGMPSYGGLAGRDME AMAIGLREAMQYEYIEHRVKQVRYLGDKLKAAGVPIVEPVGGHAVFLDARRFCEHLTQDE FPAQSLAASIYVETGVRSMERGIISAGRNNVTGEHHRPKLETVRLTIPRRVYTYAHMDVV ADGIIKLYQHKEDIRGLKFIYEPKQLRFFTARFDYI
- Number of residues
- 456
- Molecular Weight
- 51499.525
- Theoretical pI
- 6.28
- GO Classification
- Functionstyrosine phenol-lyase activityProcessestyrosine metabolic process
- General Function
- Tyrosine phenol-lyase activity
- Specific Function
- Not Available
- Pfam Domain Function
- Beta_elim_lyase (PF01212)
- Transmembrane Regions
- Not Available
- Cellular Location
- Not Available
- Gene sequence
>lcl|BSEQ0007858|1371 bp ATGAATTATCCGGCAGAACCCTTCCGTATTAAAAGCGTTGAAACTGTATCTATGATCCCG CGTGATGAACGCCTCAAGAAAATGCAGGAAGCGGGTTACAATACTTTCCTGTTAAATTCG AAAGATATTTATATTGACCTGCTGACAGACAGTGGCACTAACGCAATGAGCGACAAGCAG TGGGCCGGAATGATGATGGGTGATGAAGCGTACGCGGGCAGCGAAAACTTCTATCATCTG GAAAGAACCGTGCAGGAACTGTTTGGCTTTAAACATATTGTTCCGACTCACCAGGGGCGT GGCGCAGAAAACCTGTTATCGCAGCTGGCTATTAAACCTGGGCAATATGTTGCCGGGAAT ATGTATTTCACTACCACCCGTTATCACCAGGAAAAAAATGGTGCGGTGTTTGTCGATATC GTTCGTGACGAAGCGCACGATGCCGGTCTGAATATTGCGTTTAAAGGTGATATCGATCTT AAAAAATTACAAAAGCTGATTGATGAAAAAGGCGCAGAGAATATTGCGTATATCTGCCTT GCGGTGACGGTTAACCTCGCGGGCGGCCAACCGGTCTCGATGGCTAACATGCGTGCGGTG CGTGAACTGACAGAAGCGCATGGCATTAAAGTGTTCTACGACGCTACCCGCTGCGTAGAA AACGCCTACTTTATCAAAGAGCAAGAGCAGGGCTTTGAGAACAAGAGCATCGCCGAGATC GTGCATGAGATGTTCAGCTACGCCGACGGTTGTACCATGAGTGGTAAAAAAGACTGTCTG GTGAACATCGGCGGCTTCCTGTGCATGAACGATGACGAAATGTTCTCTTCTGCCAAAGAG TTAGTCGTGGTCTACGAAGGGATGCCATCTTACGGCGGCCTGGCCGGACGTGATATGGAA GCGATGGCGATTGGCCTGCGTGAAGCCATGCAGTACGAATATATTGAGCACCGCGTGAAG CAGGTTCGCTACCTGGGCGATAAGCTGAAAGCCGCTGGCGTACCGATTGTTGAACCGGTA GGCGGTCACGCGGTATTCCTCGATGCGCGTCGCTTCTGCGAGCATCTGACGCAAGATGAG TTCCCGGCACAAAGTCTGGCTGCCAGCATCTATGTGGAAACCGGCGTGCGCAGTATGGAG CGCGGAATTATCTCTGCGGGCCGTAATAACGTGACCGGTGAACACCACAGACCGAAACTG GAAACCGTGCGTCTGACTATTCCACGTCGTGTTTATACCTACGCACATATGGATGTTGTG GCTGACGGTATTATTAAACTTTACCAGCACAAAGAAGATATTCGCGGGCTGAAGTTTATT TACGAGCCGAAGCAGTTGCGTTTCTTTACTGCACGCTTTGATTACATCTAA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P31013 UniProtKB Entry Name TPL_CITFR GenBank Protein ID 40482 GenBank Gene ID X66978 - General References
- Antson AA, Demidkina TV, Gollnick P, Dauter Z, von Tersch RL, Long J, Berezhnoy SN, Phillips RS, Harutyunyan EH, Wilson KS: Three-dimensional structure of tyrosine phenol-lyase. Biochemistry. 1993 Apr 27;32(16):4195-206. [Article]
- Antson AA, Strokopytov BV, Murshudov GN, Isupov MN, Harutyunyan EH, Demidkina TV, Vassylyev DG, Dauter Z, Terry H, Wilson KS: The polypeptide chain fold in tyrosine phenol-lyase, a pyridoxal-5'-phosphate-dependent enzyme. FEBS Lett. 1992 May 18;302(3):256-60. [Article]
- Sundararaju B, Antson AA, Phillips RS, Demidkina TV, Barbolina MV, Gollnick P, Dodson GG, Wilson KS: The crystal structure of Citrobacter freundii tyrosine phenol-lyase complexed with 3-(4'-hydroxyphenyl)propionic acid, together with site-directed mutagenesis and kinetic analysis, demonstrates that arginine 381 is required for substrate specificity. Biochemistry. 1997 May 27;36(21):6502-10. [Article]