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 residues388
Molecular Weight43592.715
Theoretical pI7.11
GO Classification
Functions
  • pyridoxal phosphate binding
  • alanine racemase activity
Processes
  • D-alanine biosynthetic process
General FunctionPyridoxal phosphate binding
Specific FunctionCatalyzes the interconversion of L-alanine and D-alanine. Also weakly active on serine.
Pfam Domain Function
Transmembrane RegionsNot Available
GenBank Protein ID142467
UniProtKB IDP10724
UniProtKB Entry NameALR_GEOSE
Cellular LocationNot 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
GenBank Gene IDM19142
GeneCard IDNot Available
GenAtlas IDNot Available
HGNC IDNot Available
Chromosome LocationNot Available
LocusNot Available
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