학술논문

X-ray analysis of two antibiotic-synthesizing bacterial ester hydrolases: preliminary results.
Document Type
Article
Source
Acta Crystallographica: Section D (Wiley-Blackwell). Jan2003, Vol. 59 Issue 1, p158. 3p.
Subject
*HYDROLASES
*ESTERS
*XANTHOMONAS campestris
Language
ISSN
0907-4449
Abstract
α-Amino-acid ester hydrotases are multimeric enzymes of potential use in antibiotic production. Knowledge of their structure could help to engineer these enzymes into economically viable biocatalysts. The α-amino-acid ester hydrolases from Xanthomonas citri and Acetobacter turbidans have been crystallized. The X. cirri enzyme crystallizes in a primitive monoclinic space group (unit-cell parameters a = 90.1, b = 125.8, c = 132.1 Å, β = 90.9°). The A. turbidans enzyme crystallizes in both a primitive orthorhombic (a = 99.1, b = 104.9, c = 284.9 Å) and a body-centred cubic space group with a = b = c = 342.2 Å. From both enzymes, diffractionquality crystals (resolution 3.0 Å or better) were obtained. Datacollection statistics are reported for data sets from both enzymes. [ABSTRACT FROM AUTHOR]