Document Detail

Identification and biochemical characterization of a thermostable malate dehydrogenase from the mesophile Streptomyces coelicolor A3(2).
MedLine Citation:
PMID:  21071865     Owner:  NLM     Status:  MEDLINE    
We identified and characterized a malate dehydrogenase from Streptomyces coelicolor A3(2) (ScMDH). The molecular mass of ScMDH was 73,353.5 Da with two 36,675.0 Da subunits as analyzed by matrix-assisted laser-desorption ionization-time-of-flight mass spectrometry (MALDI-TOF-MS). The detailed kinetic parameters of recombinant ScMDH are reported here. Heat inactivation studies showed that ScMDH was more thermostable than most MDHs from other organisms, except for a few extremely thermophile bacteria. Recombinant ScMDH was highly NAD(+)-specific and displayed about 400-fold (k(cat)) and 1,050-fold (k(cat)/K(m)) preferences for oxaloacetate reduction over malate oxidation. Substrate inhibition studies showed that ScMDH activity was inhibited by excess oxaloacetate (K(i)=5.8 mM) and excess L-malate (K(i)=12.8 mM). Moreover, ScMDH activity was not affected by most metal ions, but was strongly inhibited by Fe(2+) and Zn(2+). Taken together, our findings indicate that ScMDH is significantly thermostable and presents a remarkably high catalytic efficiency for malate synthesis.
Ya-Dong Ge; Zheng-Yu Cao; Zong-Da Wang; Lu-Lu Chen; You-Ming Zhu; Guo-Ping Zhu
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2010-11-07
Journal Detail:
Title:  Bioscience, biotechnology, and biochemistry     Volume:  74     ISSN:  1347-6947     ISO Abbreviation:  Biosci. Biotechnol. Biochem.     Publication Date:  2010  
Date Detail:
Created Date:  2010-11-30     Completed Date:  2011-03-23     Revised Date:  2011-08-11    
Medline Journal Info:
Nlm Unique ID:  9205717     Medline TA:  Biosci Biotechnol Biochem     Country:  Japan    
Other Details:
Languages:  eng     Pagination:  2194-201     Citation Subset:  IM    
Key Laboratory of Molecular Evolution and Biodiversity and Institute of Molecular Biology and Biotechnology, and Key Laboratory of the Biotic Environment and Ecological Safety in Anhui Province, Anhui Normal University, Wuhu, China.
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MeSH Terms
Enzyme Inhibitors
Enzyme Stability
Hot Temperature*
Malate Dehydrogenase / metabolism*
Malates / metabolism
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Streptomyces coelicolor / enzymology*
Reg. No./Substance:
0/Enzyme Inhibitors; 0/Malates; 53-84-9/NAD; 6915-15-7/malic acid; EC Dehydrogenase

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

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