NDLI: Expression and identification of a thermostable malate dehydrogenase from multicellular prokaryote Streptomyces avermitilis MA-4680

Content Provider	Springer Nature Link
Author	Wang, Zong Da Wang, Bao Juan Ge, Ya Dong Pan, Wei Wang, Jie Xu, Lei Liu, Ai Min Zhu, Guo Ping
Copyright Year	2010
Abstract	A malate dehydrogenase (MDH) from Streptomyces avermitilis MA-4680 (SaMDH) has been expressed and purified as a fusion protein. The molecular mass of SaMDH is about 35 kDa determined by SDS-PAGE. The recombinant SaMDH has a maximum activity at pH 8.0. The enzyme shows the optimal temperature around 42°C and displays a half-life (t $_{1/2}$) of 160 min at 50°C which is more thermostable than reported MDHs from most bacteria and fungi. The k $_{cat}$ value of SaMDH is about 240-fold of that for malate oxidation. In addition, the k $_{cat}$/K $_{m}$ ratio shows that SaMDH has about 1,246-fold preference for oxaloacetate (OAA) reduction over l-malate oxidation. The recombinant SaMDH may also use NADPH as a cofactor although it is a highly NAD(H)-specific enzyme. There was no activity detected when malate and NADP$^{+}$ were used as substrates. Substrate inhibition studies show that SaMDH activity is strongly inhibited by excess OAA with NADH, but is not sensitive to excess l-malate. Enzymatic activity is enhanced by the addition of Na$^{+}$, NH$_{4}$ $^{+}$, Ca$^{2+}$, Cu$^{2+}$ and Mg$^{2+}$ and inhibited by addition of Hg$^{2+}$ and Zn$^{2+}$. MDH is widely used in coenzyme regeneration, antigen immunoassays and bioreactors. The enzymatic analysis could provide the important basic knowledge for its utilizations.
Starting Page	1629
Ending Page	1636
Page Count	8
File Format	PDF
ISSN	03014851
Journal	Molecular Biology Reports
Volume Number	38
Issue Number	3
e-ISSN	15734978
Language	English
Publisher	Springer Netherlands
Publisher Date	2010-09-16
Publisher Place	Dordrecht
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Streptomyces avermitilis MA-4680 Malate dehydrogenase Thermostability Enzymatic characterization Coenzyme specificity Animal Biochemistry Animal Anatomy / Morphology / Histology
Content Type	Text
Resource Type	Article
Subject	Genetics Medicine Molecular Biology

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