Crystallization and X-ray structure analysis of a thermostable penicillin G acylase from alcaligenes faecalis

TitleCrystallization and X-ray structure analysis of a thermostable penicillin G acylase from alcaligenes faecalis
Publication TypeJournal Article
Year of Publication2012
AuthorsVarshney, NKumar, R. Kumar, S, Ignatova, Z, Prabhune, A, Pundle, A, Dodson, EJ, Suresh, CG
JournalActa Crystallographica Section F-Structural Biology and Crystallization Communications
Volume68
Pagination273-277
Date PublishedMAR
ISSN1744-3091
Keywordscalcium binding, disulfide bridges, Ntn hydrolases, orthorhombic form, tetragonal form, Thermostability
Abstract

{The enzyme penicillin G acylase (EC 3.5.1.11) catalyzes amide-bond cleavage in benzylpenicillin (penicillin G) to yield 6-aminopenicillanic acid, an intermediate chemical used in the production of semisynthetic penicillins. A thermostable penicillin G acylase from Alcaligenes faecalis (AfPGA) has been crystallized using the hanging-drop vapour-diffusion method in two different space groups: C2221, with unit-cell parameters a = 72.9
DOI10.1107/S1744309111053930
Type of Journal (Indian or Foreign)Foreign
Impact Factor (IF)0.552
Divison category: 
Biochemical Sciences