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Kolattukudy, P E,Kim , Yu Sam,Flurkey, W H 생화학분자생물학회 1987 BMB Reports Vol.14 No.4
Malonyl-CoA decarboxylase, a mitochondrial 47 K dalton peptide, is translated as a 50 K dalton peptide. Evidence is presented that in the preen gland of goose this 50 K dalton unprocessed peptide accumulates in the cytoplasm, where the catalytic activity of this precursor performs a biological function. This is the first case of cytoplasmic accumulation of a catalytically active precursor form of a mitochondrial enzyme.
Microbial Malonyl - CoA Decarboxylase
Kim, Yu Sam,Kolattukudy, P. E. 생화학분자생물학회 1985 BMB Reports Vol.12 No.4
Malonyl-CoA decarboxylase was partially purified from Mycobacterium tuberculossi H37Ra. The molecular weight of the enzyme was 44,000 and the pI and pH optimum (were 6.7 and 5.5, respectively. The enzyme showed a typical Michaelis-Menten substrate saturation, with an apparent Km and V of 0.2mM and 3. 85μ㏖/min/㎎, respectively. It catalyzed decarboxylation of methylmaonyl-CoA only at 5% of the rate observed with malonyl-CoA, whereas malonic acid and succinyl-CoA were not decarboxylated. Antibodies prepared against malonyl-CoA decarboxylase from the uropygial glands of goose and rat liver mitochondria did not inhibit the bacterial enzyme. Avidin did not inhibit the enzyme suggesting that biotin was not involved in the reaction. Thiol-directed reagents inhibited the enzyme as did CoA, acetyl-CoA, propionyl-CoA, methylmalonyl-CoA, and succinyl-CoA. Malonyl-CoA decarboxylase was also partially purified from malonategrown Pseudomonas fluorescens. The molecular weight of this enzyme was 56,000 and the pH optimum and apparent Km were 5.5 and 1mM, respectively. Unlike the mycobacterial enzyme, this enzyme was insensitive to p-hydroxymercuribenzoate, acetyl-CoA, and propionyl-CoA, and it was less sensitive to inhibition by succinyl-CoA and CoA than the mycobacterial enzyme. The size and properties of the two bacterial enzymes suggest that these are quite unlike the mammalian and avian enzymes and that they constitute a different class of malonyl-CoA decarboxylases.
Lee, Kil-Soo,Dubey, Vinod S.,Kolattukudy, Pappachan E.,Song, Chang-Hwa,Shin, A-Rum,Jung, Saet-Byel,Yang, Chul-Su,Kim, Su-Young,Jo, Eun-Kyeong,Park, Jeong-Kyu,Kim, Hwa-Jung Published by Elsevier/North Holland on behalf of t 2007 FEMS microbiology letters Vol.267 No.1
<P>The lipids located in the outer layer of Mycobacterium tuberculosis, which include sulfolipid, phthiocerol dimycocerosate (PDIM), diacyltrehalose, and polyacyltrehalose, may play a role in host-pathogen interactions. These lipids were purified using thin-layer chromatography, and their ability to induce proinflammatory cytokines in human monocytes and in a human acute monocytic leukemia cell line (THP-1) was examined. None of the lipids tested induced significant interleukin (IL)-12p40 or tumor necrosis factor (TNF)-alpha production in monocytic cells. Diacyltrehalose significantly inhibited lipopolysaccharide- and M. tuberculosis-induced IL-12p40, TNF-alpha, and IL-6 productions in human monocytes, whereas other lipids had no effect. However, diacyltrehalose was unable to inhibit peptidoglycan-induced IL-12p40 production. These results suggest that diacyltrehalose is a mycobacterial factor capable of modulating host immune responses.</P>