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| MOLECULAR-STRUCTURE OF THE ACYL-ENZYME INTERMEDIATE IN BETA-LACTAM HYDROLYSIS AT 1.7 ANGSTROM RESOLUTION |
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| Author(s): STRYNADKA NCJ, ADACHI H, JENSEN SE, JOHNS K, SIELECKI A, BETZEL C, SUTOH K, JAMES MNG |
| Source: NATURE Volume: 359 Issue: 6397 Pages: 700-705 Published: OCT 22 1992 |
| Times Cited: 403 References: 49 |
| Abstract: The X-ray crystal structure of the molecular complex of penicillin G with a deacylation-defective mutant of the RTEM-1 beta-lactamase from Escherichia coli shows how these antibiotics are recognized and destroyed. Penicillin G is covalently bound to Ser 70 O(gamma) as an acyl-enzyme intermediate. The deduced catalytic mechanism uses Ser 70 O(gamma) as the attacking nucleophile during acylation. Lys 73 N(zeta) acts as a general base in abstracting a proton from Ser 70 and transferring it to the thiazolidine ring nitrogen atom via Ser 130 O(gamma). Deacylation is accomplished by nucleophilic attack on the penicilloyl carbonyl carbon by a water molecule assisted by the general base, Glu 166. |
| Document Type: Article |
| Language: English |
Addresses:
1. UNIV ALBERTA, DEPT BIOCHEM, MRC, PROT STRUCT & FUNCT GRP, EDMONTON T6G 2H7, ALBERTA CANADA
2. DESY, EUROPEAN MOLEC BIOL LAB, W-2000 HAMBURG 52, GERMANY
3. UNIV ALBERTA, DEPT MICROBIOL, EDMONTON T6G 2E9, ALBERTA CANADA
4. UNIV TOKYO, COLL ARTS & SCI, DEPT PURE & APPL SCI, MEGURO KU, TOKYO 153, JAPAN |
| Publisher: MACMILLAN MAGAZINES LTD, PORTERS SOUTH, 4 CRINAN ST, LONDON, ENGLAND N1 9XW |
| Subject Category: Multidisciplinary Sciences |
| IDS Number: JU650 |
| ISSN: 0028-0836 |
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