Priyadarshi, Amit Lee, Eun Hye Sung, Min Woo Kim, Jae-Hee Ku, Min-Je Kim, Eunice Eunkyeong Hwang, Kwang Yeon 2024-01-21T00:02:28Z 2024-01-21T00:02:28Z 2021-09-02 2008-01 1017-7825 https://pubs.kist.re.kr/handle/201004/133857 Alanine racemase, a bacterial enzyme belonging to the fold-type III group of pyridoxal 5'-phosphate (PLP)-dependent enzymes, has been shown to catalyze the interconversion between L- and D-alanine. The alanine racemase from the pathogenic bacterium Enterococcus faecalis v583 has been overexpressed in E. coli and was shown to crystallize an enzyme at 295 K, using polyethylene glycol (PEG) 8000 as a precipitant. X-ray diffraction data to 2.5 angstrom has been collected using synchrotron radiation. The crystal is a member of the orthorhombic space group, C222(1), with unit cell parameter of a=94.634, b=156.516, c=147.878 angstrom, and alpha=beta=gamma=90 degrees. Two or three monomers are likely to be present in the asymmetric unit, with a corresponding V,, of 3.38 angstrom(3) Da(-1) and 2.26 angstrom(3) Da(-1) and a solvent content of 63.7% and 45.5%, respectively. English KOREAN SOC MICROBIOLOGY & BIOTECHNOLOGY INFECTION Overexpression, crystallization, and preliminary x-ray crystallographic analysis of the alanine racemase from Enterococcus faecalis v583 Article 1 JOURNAL OF MICROBIOLOGY AND BIOTECHNOLOGY, v.18, no.1, pp.55 - 58 JOURNAL OF MICROBIOLOGY AND BIOTECHNOLOGY 18 1 55 58 scie scopus kci ART001225122 000254047600008 2-s2.0-43749118758 Biotechnology & Applied Microbiology Microbiology Biotechnology & Applied Microbiology Microbiology Article INFECTION alanine racemase PLP Enterococcus faecalis preliminary x-ray analysis