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| THE METAL-ION FREE OXIDOREDUCTASE FROM STREPTOMYCES-AUREOFACIENS HAS AN ALPHA/BETA HYDROLASE FOLD |
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| Author(s): HECHT HJ, SOBEK H, HAAG T, PFEIFER O, VANPEE KH |
| Source: NATURE STRUCTURAL BIOLOGY Volume: 1 Issue: 8 Pages: 532-537 Published: AUG 1994 |
| Times Cited: 96 References: 30 |
| Abstract: The crystal structure of the bromoperoxidase A2 from Streptomyces aureofaciens (ATCC 10762) has been determined by isomorphous replacement and refined to 2.05 Angstrom resolution with an R-value of 18.4%. The enzyme catalyzes the bromination of organic compounds in the presence of bromide and peroxide. The structure confirms the absence of cofactors such as metal ions or haem groups and shows the general topology of the alpha/beta hydrolase fold. The active centre is at the end of a deep pocket and includes a catalytic triad of Ser 98, Asp 228 and His 257. The active centre is connected by a narrow tunnel to a second pocket on the enzyme surface. |
| Document Type: Article |
| Language: English |
| Reprint Address: HECHT, HJ (reprint author), GBF, DEPT MOLEC STRUCT RES, MASCHERODER WEG 1, D-38124 BRAUNSCHWEIG, GERMANY |
Addresses:
1. UNIV HOHENHEIM, INST MICROBIOL, D-70593 STUTTGART, GERMANY
2. TECH UNIV DRESDEN, DEPT BIOCHEM, D-01062 DRESDEN, GERMANY |
| Publisher: NATURE PUBLISHING CO, 345 PARK AVE SOUTH, NEW YORK, NY 10010-1707 |
| Subject Category: Biochemistry & Molecular Biology; Biophysics; Cell Biology |
| IDS Number: QR967 |
| ISSN: 1072-8368 |
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| | | | | | | | | Record from Web of Science® | | | | | | | | | |