Literature: Alanine racemase, N-terminal (IPR001608)
References used in this entry
The following publications were referred to in the abstract:
Determination of the structure of alanine racemase from Bacillus stearothermophilus at 1.9-A resolution.
Shaw JP, Petsko GA, Ringe D.
Biochemistry 36 1329-42 1997
PMID: 9063881 Related citations
The following publications were not referred to in the abstract, but provide useful additional information:
Effect of a Y265F mutant on the transamination-based cycloserine inactivation of alanine racemase.
Fenn TD, Holyoak T, Stamper GF, Ringe D.
Biochemistry 44 5317-27 2005
PMID: 15807525 Related citations
Self-protection mechanism in D-cycloserine-producing Streptomyces lavendulae. Gene cloning, characterization, and kinetics of its alanine racemase and D-alanyl-D-alanine ligase, which are target enzymes of D-cycloserine.
Noda M, Kawahara Y, Ichikawa A, Matoba Y, Matsuo H, Lee DG, Kumagai T, Sugiyama M.
J. Biol. Chem. 279 46143-52 2004
PMID: 15302885 Related citations
Structures of an alanine racemase from Bacillus anthracis (BA0252) in the presence and absence of (R)-1-aminoethylphosphonic acid (L-Ala-P).
Au K, Ren J, Walter TS, Harlos K, Nettleship JE, Owens RJ, Stuart DI, Esnouf RM.
Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 64 327-33 2008
PMID: 18453697 Related citations
The 1.9 A crystal structure of alanine racemase from Mycobacterium tuberculosis contains a conserved entryway into the active site.
LeMagueres P, Im H, Ebalunode J, Strych U, Benedik MJ, Briggs JM, Kohn H, Krause KL.
Biochemistry 44 1471-81 2005
PMID: 15683232 Related citations
Structural evidence that alanine racemase from a D-cycloserine-producing microorganism exhibits resistance to its own product.
Noda M, Matoba Y, Kumagai T, Sugiyama M.
J. Biol. Chem. 279 46153-61 2004
PMID: 15302886 Related citations