| Literature DB >> 10398370 |
H Munier-Lehmann1, S Burlacu-Miron, C T Craescu, H H Mantsch, C P Schultz.
Abstract
The adk gene from Mycobacterium tuberculosis codes for an enzyme of 181 amino acids. A sequence comparison with 52 different forms of adenylate kinases (AK) suggests that the enzyme from M. tuberculosis belongs to a new subfamily of "short" bacterial AKs. The recombinant protein, overexpressed in Escherichia coli, exhibits a low catalytic activity and an unexpectedly high thermal stability (Tm = 64.8 degrees C). Based on various spectroscopic data, on the known three-dimensional structure of the AK from E. coli and on secondary structure predictions for various sequenced AKs, we propose a structural model for AK from M. tuberculosis (AKmt). Proteins 1999;36:238-248. Copyright 1999 Wiley-Liss, Inc.Entities:
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Year: 1999 PMID： 10398370
Source DB: PubMed Journal: Proteins ISSN： 0887-3585