Role of protein subunits in Proteus rettgeri penicillin G acylase
نویسندگان
چکیده
منابع مشابه
Expression and regulation of the penicillin G acylase gene from Proteus rettgeri cloned in Escherichia coli.
The penicillin G acylase genes from the Proteus rettgeri wild type and from a hyperproducing mutant which is resistant to succinate repression were cloned in Escherichia coli K-12. Expression of both wild-type and mutant P. rettgeri acylase genes in E. coli K-12 was independent of orientation in the cloning vehicle and apparently resulted from recognition in E. coli of the P. rettgeri promoter ...
متن کاملCrystal structure of penicillin G acylase from the Bro1 mutant strain of Providencia rettgeri.
Penicillin G acylase is an important enzyme in the commercial production of semisynthetic penicillins used to combat bacterial infections. Mutant strains of Providencia rettgeri were generated from wild-type cultures subjected to nutritional selective pressure. One such mutant, Bro1, was able to use 6-bromohexanamide as its sole nitrogen source. Penicillin acylase from the Bro1 strain exhibited...
متن کاملacylase from Providencia rettgeri
Two isoforms of the heterodimeric enzyme penicillin G acylase (EC 3.5.1.1 I ) from Providencia rettgeri ATCC 31052 (strain Brol) were purified to near homogeneity. The isoforms exhibited comparable enzymatic a tivities but differed slightly in the molecular weight and PI of their respective a-subunit. The origin of this difference was traced to the partial conversion of the N-terminal Gln of th...
متن کاملProtein Engineering of Penicillin Acylase
Penicillin acylases (PA) are widely used for the production of semi-synthetic β-lactam antibiotics and chiral compounds. In this review, the latest achievements in the production of recombinant enzymes are discussed, as well as the results of PA type G protein engineering.
متن کاملBiotypes of Proteus rettgeri.
Examination of 729 isolates of Proteus rettgeri showed that 674 reacted positively in tests for phenylalanine deamination, indole production, growth on citrate, and acid production from meso-inositol, and negatively for L-ornithine decarboxylation and acid production from lactose, maltose, D-xylose, and L-arabinose. Only 51 isolates differed in one, and four differed in two of these ten reactio...
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ژورنال
عنوان ژورنال: Journal of Bacteriology
سال: 1985
ISSN: 0021-9193,1098-5530
DOI: 10.1128/jb.163.3.1279-1281.1985