Alanine racemase

NameAlanine racemase
Synonyms
  • 5.1.1.1
  • dal
Gene Namealr
OrganismGeobacillus stearothermophilus
Amino acid sequence
>lcl|BSEQ0010938|Alanine racemase
MNDFHRDTWAEVDLDAIYDNVENLRRLLPDDTHIMAVVKANAYGHGDVQVARTALEAGAS
RLAVAFLDEALALREKGIEAPILVLGASRPADAALAAQQRIALTVFRSDWLEEASALYSG
PFPIHFHLKMDTGMGRLGVKDEEETKRIVALIERHPHFVLEGLYTHFATADEVNTDYFSY
QYTRFLHMLEWLPSRPPLVHCANSAASLRFPDRTFNMVRFGIAMYGLAPSPGIKPLLPYP
LKEAFSLHSRLVHVKKLQPGEKVSYGATYTAQTEEWIGTIPIGYADGWLRRLQHFHVLVD
GQKAPIVGRICMDQCMIRLPGPLPVGTKVTLIGRQGDEVISIDDVARHLETINYEVPCTI
SYRVPRIFFRHKRIMEVRNAIGRGESSA
Number of residuesNone
Molecular Weight43592.715
Theoretical pI7.11
GO Classification
Functions
  • pyridoxal phosphate binding
  • alanine racemase activity
Processes
  • D-alanine biosynthetic process
Components
General FunctionPyridoxal phosphate binding
Specific FunctionCatalyzes the interconversion of L-alanine and D-alanine. Also weakly active on serine.
Transmembrane Regions
GenBank Protein ID
UniProtKB IDP10724
UniProtKB Entry Name
Cellular LocationNone
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
GenBank Gene ID
GeneCard IDNone
GenAtlas ID
HGNC ID
Chromosome LocationNone
LocusNone
References
  1. 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. [2835089 ]
  2. Faraci WS, Walsh CT: Mechanism of inactivation of alanine racemase by beta, beta, beta-trifluoroalanine. Biochemistry. 1989 Jan 24;28(2):431-7. [2496744 ]
  3. 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. [3730360 ]
  4. 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. [10194319 ]
  5. 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. [10502689 ]
  6. 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. [12203980 ]
  7. 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. [9063881 ]
  8. 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. [9671513 ]
  9. 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. [10079072 ]
  10. 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. [11886871 ]
  11. 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. [12741835 ]
  12. 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. [15807525 ]

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