Alanine racemase
Details
- Name
- Alanine racemase
- Synonyms
- 5.1.1.1
- dal
- Gene Name
- alr
- Organism
- Geobacillus stearothermophilus
- Amino acid sequence
>lcl|BSEQ0010938|Alanine racemase MNDFHRDTWAEVDLDAIYDNVENLRRLLPDDTHIMAVVKANAYGHGDVQVARTALEAGAS RLAVAFLDEALALREKGIEAPILVLGASRPADAALAAQQRIALTVFRSDWLEEASALYSG PFPIHFHLKMDTGMGRLGVKDEEETKRIVALIERHPHFVLEGLYTHFATADEVNTDYFSY QYTRFLHMLEWLPSRPPLVHCANSAASLRFPDRTFNMVRFGIAMYGLAPSPGIKPLLPYP LKEAFSLHSRLVHVKKLQPGEKVSYGATYTAQTEEWIGTIPIGYADGWLRRLQHFHVLVD GQKAPIVGRICMDQCMIRLPGPLPVGTKVTLIGRQGDEVISIDDVARHLETINYEVPCTI SYRVPRIFFRHKRIMEVRNAIGRGESSA
- Number of residues
- 388
- Molecular Weight
- 43592.715
- Theoretical pI
- 7.11
- GO Classification
- Functionsalanine racemase activity / pyridoxal phosphate bindingProcessesD-alanine biosynthetic process
- General Function
- Pyridoxal phosphate binding
- Specific Function
- Catalyzes the interconversion of L-alanine and D-alanine. Also weakly active on serine.
- Pfam Domain Function
- Transmembrane Regions
- Not Available
- Cellular Location
- Not Available
- Gene sequence
>lcl|BSEQ0002668|1161 bp ATGAACGACTTTCATCGCGATACGTGGGCGGAAGTGGATTTGGACGCCATTTACGACAAT GTGGAGAATTTGCGCCGTTTGCTGCCGGACGACACGCACATTATGGCGGTCGTGAAAGCG AACGCCTATGGACATGGGGATGTGCAGGTGGCAAGGACAGCGCTCGAACGGGGGCCTCCG CCTGCGGTTGCCTTTTTGGATGAGGCGCTCGCTTTAAGGGAAAAAGGAATCGAAGCGCCG ATTCTAGTTCTCGGGGCTTCCCGTCCAGCTGATGCGGCGCTGGCCGCCCAGCAGCGCATT GCCCTGACCGTGTTCCGCTCCGACTGGTTGGAAGAAGCGTCCGCCCTTTACAGCGGCCCT TTTCCTATTCATTTCCATTTGAAAATGGACACCGGCATGGGACGGCTTGGAGTGAAAGAC GAGGAAGAGACGAAACGAATCGTAGCGCTGATTGAGCGCCATCCGCATTTTGTGCTTGAA GGGTTGTACACGCATTTTGCGACTGCGGATGAGGTGAACACCGATTATTTTTCCTATCAG TATACCCGTTTTTTGCACATGCTCGAATGGCTGCCGTCGCGCCCGCCGCTCGTCCATTGC GCCAACAGCGCAGCGTCGCTCCGTTTCCCTGACCGGACGTTCAATATGGTCCGCTTCGGC ATTGCCATGTATGGGCTTGCCCCGTCGCCCGGCATCAAGCCGCTGCTGCCGTATCCATTA AAAGAAGCATTTTCGCTCCATAGCCGCCTCGTACACGTCAAAAAACTGCAACCAGGCGAA AAGGTGAGCTATGGTGCGACGTACACTGCGCAGACGGAGGAGTGGATCGGGACGATTCCG ATCGGCTATGCGGACGGCGTCCGCCGCCTGCAGCACTTTCATGTCCTTGTTGACGGACAA AAGGCGCCGATTGTCGGCCGCATTTGCATGGACCAGTGCATGATCCGCCTGCCTGGTCCG CTGCCGGTCGGCACGAAGGTGACACTGATTGGTCGCCAAGGGGACGAGGTAATTTCCATT GATGATGTCGCTCGCCATTTGGAAACGATCAACTACGAAGTGCCTTGCACGATCAGTTAT CGAGTGCCCCGTATTTTTTTCCGCCATAAGCGTATAATGGAAGTGAGAAACGCCATTGGC CGCGGGGAAAGCAGTGCATAA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P10724 UniProtKB Entry Name ALR_GEOSE GenBank Protein ID 142467 GenBank Gene ID M19142 - General References
- Tanizawa K, Ohshima A, Scheidegger A, Inagaki K, Tanaka H, Soda K: Thermostable alanine racemase from Bacillus stearothermophilus: DNA and protein sequence determination and secondary structure prediction. Biochemistry. 1988 Feb 23;27(4):1311-6. [Article]
- Faraci WS, Walsh CT: Mechanism of inactivation of alanine racemase by beta, beta, beta-trifluoroalanine. Biochemistry. 1989 Jan 24;28(2):431-7. [Article]
- Badet B, Inagaki K, Soda K, Walsh CT: Time-dependent inhibition of Bacillus stearothermophilus alanine racemase by (1-aminoethyl)phosphonate isomers by isomerization to noncovalent slowly dissociating enzyme-(1-aminoethyl)phosphonate complexes. Biochemistry. 1986 Jun 3;25(11):3275-82. [Article]
- Sun S, Toney MD: Evidence for a two-base mechanism involving tyrosine-265 from arginine-219 mutants of alanine racemase. Biochemistry. 1999 Mar 30;38(13):4058-65. [Article]
- Watanabe A, Yoshimura T, Mikami B, Esaki N: Tyrosine 265 of alanine racemase serves as a base abstracting alpha-hydrogen from L-alanine: the counterpart residue to lysine 39 specific to D-alanine. J Biochem. 1999 Oct;126(4):781-6. [Article]
- Patrick WM, Weisner J, Blackburn JM: Site-directed mutagenesis of Tyr354 in Geobacillus stearothermophilus alanine racemase identifies a role in controlling substrate specificity and a possible role in the evolution of antibiotic resistance. Chembiochem. 2002 Aug 2;3(8):789-92. [Article]
- Shaw JP, Petsko GA, Ringe D: Determination of the structure of alanine racemase from Bacillus stearothermophilus at 1.9-A resolution. Biochemistry. 1997 Feb 11;36(6):1329-42. [Article]
- Stamper GF, Morollo AA, Ringe D: Reaction of alanine racemase with 1-aminoethylphosphonic acid forms a stable external aldimine. Biochemistry. 1998 Jul 21;37(29):10438-45. [Article]
- Morollo AA, Petsko GA, Ringe D: Structure of a Michaelis complex analogue: propionate binds in the substrate carboxylate site of alanine racemase. Biochemistry. 1999 Mar 16;38(11):3293-301. [Article]
- Watanabe A, Yoshimura T, Mikami B, Hayashi H, Kagamiyama H, Esaki N: Reaction mechanism of alanine racemase from Bacillus stearothermophilus: x-ray crystallographic studies of the enzyme bound with N-(5'-phosphopyridoxyl)alanine. J Biol Chem. 2002 May 24;277(21):19166-72. Epub 2002 Mar 8. [Article]
- Fenn TD, Stamper GF, Morollo AA, Ringe D: A side reaction of alanine racemase: transamination of cycloserine. Biochemistry. 2003 May 20;42(19):5775-83. [Article]
- Fenn TD, Holyoak T, Stamper GF, Ringe D: Effect of a Y265F mutant on the transamination-based cycloserine inactivation of alanine racemase. Biochemistry. 2005 Apr 12;44(14):5317-27. [Article]
Drug Relations
- Drug Relations
DrugBank ID Name Drug group Pharmacological action? Actions Details DB01993 N-(5'-Phosphopyridoxyl)-D-Alanine experimental unknown Details DB02142 Pyridoxamine-5'-Phosphate experimental unknown Details DB03097 PMP-hydroxyisoxazole, pyridoxamine-5-phosphate-hydroxyisoxazole experimental unknown Details DB03327 {1-[(3-Hydroxy-Methyl-5-Phosphonooxy-Methyl-Pyridin-4-Ylmethyl)-Amino]-Ethyl}-Phosphonic Acid experimental unknown Details DB02038 D-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl]-N,O-cycloserylamide experimental unknown Details DB03766 Propanoic acid approved, vet_approved unknown Details DB03801 Lysine Nz-Carboxylic Acid experimental unknown Details DB04467 N-(5'-phosphopyridoxyl)-L-alanine experimental unknown Details