Document Detail


Kinetic, mutagenic, and structural homology analysis of L-serine dehydratase from Legionella pneumophila.
MedLine Citation:
PMID:  21878319     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
A structural database search has revealed that the same fold found in the allosteric substrate binding (ASB) domain of Mycobacterium tuberculosis D-3-phosphoglycerate dehydrogenase (PGDH) is found in l-serine dehydratase from Legionella pneumophila. The M. tuberculosis PGDH ASB domain functions in the control of catalytic activity. Bacterial l-serine dehydratases are 4Fe-4S proteins that convert l-serine to pyruvate and ammonia. Sequence homology reveals two types depending on whether their α and β domains are on the same (Type 2) or separate (Type 1) polypeptides. The α domains contain the catalytic iron-sulfur center while the β domains do not yet have a described function, but the structural homology with PGDH suggests a regulatory role. Type 1 β domains also contain additional sequence homologous to PGDH ACT domains. A continuous assay for l-serine dehydratase is used to demonstrate homotropic cooperativity, a broad pH range, and essential irreversibility. Product inhibition analysis reveals a Uni-Bi ordered mechanism with ammonia dissociating before pyruvate. l-Threonine is a poor substrate and l-cysteine and d-serine are competitive inhibitors with K(i) values that differ by almost 10-fold from those reported for Escherichia colil-serine dehydratase. Mutagenesis identifies the three cysteine residues at the active site that anchor the iron-sulfur complex.
Authors:
Xiao Lan Xu; Shawei Chen; Gregory A Grant
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Publication Detail:
Type:  Journal Article     Date:  2011-08-23
Journal Detail:
Title:  Archives of biochemistry and biophysics     Volume:  515     ISSN:  1096-0384     ISO Abbreviation:  Arch. Biochem. Biophys.     Publication Date:  2011 Nov 
Date Detail:
Created Date:  2011-10-12     Completed Date:  2011-11-21     Revised Date:  2012-03-30    
Medline Journal Info:
Nlm Unique ID:  0372430     Medline TA:  Arch Biochem Biophys     Country:  United States    
Other Details:
Languages:  eng     Pagination:  28-36     Citation Subset:  IM    
Copyright Information:
Copyright © 2011 Elsevier Inc. All rights reserved.
Affiliation:
Department of Developmental Biology, Washington University School of Medicine, 660 S. Euclid Avenue, St. Louis, MO 63110, USA.
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Base Sequence
Catalytic Domain
DNA Primers
Hydrogen-Ion Concentration
Kinetics
L-Serine Dehydratase / antagonists & inhibitors,  chemistry,  metabolism*
Legionella pneumophila / enzymology*
Models, Molecular
Molecular Sequence Data
Mutagens*
Protein Conformation
Sequence Homology, Amino Acid
Chemical
Reg. No./Substance:
0/DNA Primers; 0/Mutagens; EC 4.3.1.17/L-Serine Dehydratase
Comments/Corrections
Erratum In:
Arch Biochem Biophys. 2012 Mar 1;519(1):66

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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