1763-10-6Relevant articles and documents
-
Vignais,Zabin
, p. 263,265 (1958)
-
Substrate Recognition and Catalytic Mechanism of the Phosphate Acyltransferase PlsX from Bacillus subtilis
Jiang, Yiping,Qin, Mingming,Guo, Zhihong
, p. 2019 - 2028 (2020)
Phosphate: acyl-acyl carrier protein (ACP) acyltransferase PlsX is a peripheral enzyme catalysing acyl transfer to orthophosphate in phospholipid synthesis. Little is known about how it recognises substrates and catalyses the acyl transfer. Here we show that its active site includes many residues lining a long, narrow gorge at the dimeric interface, two positive residues forming a positive ACP docking pad next to the interfacial gorge, and a number of strictly conserved residues significantly contributing to the catalytic activity. These findings suggest a substrate recognition mode and a catalytic mechanism that are different from those of phosphotransacetylases catalysing a similar acyl transfer reaction. The catalytic mechanism involves substrate activation and transition-state stabilization by two strictly conserved residues, Lys184 and Asn229. Another noticeable feature of the catalysis is the release of the acyl phosphate product near the membrane, which might facilitate its membrane insertion.
PROCESS FOR ACYL-TRANSFER ENZYME REACTIONS WITH ACYL- COENZYME A
-
Paragraph 0076, (2016/07/27)
The present invention relates to a method for acyltransferase reaction in which an acyl group of acyl coenzyme A is transferred to an acyl group receptor characterized in that the reaction is carried out by production and/or reproduction of acyl coenzyme A from coenzyme A in a reaction system by a chemical thioester exchange reaction with acylthioester. The present invention, wherein expensive acyl CoA is reproduced nonenzymatically in a reaction system, enables to continuously carry out acyltransferase reaction only by putting a small amount of acyl CoA with a donor and a receptor of an acyl group into a system. Accordingly, the method of the present invention can be applied to an industrial production method of various kinds of compounds including useful biological molecules and synthesis of polymers such as polyester.
Comparison of acyl-CoA synthetic activities and enantioselectivity toward 2-arylpropanoic acids in firefly luciferases
Kato, Dai-Ichiro,Yokoyama, Keisuke,Hiraishi, Yoshihiro,Takeo, Masahiro,Negoro, Seiji
experimental part, p. 1758 - 1762 (2012/02/02)
Measurement of thioesterification activities for dodecanoic acid (C12) and ketoprofen was done using five firefly luciferases, from Pyrocoelia miyako (PmL), Photinus pyralis (PpL), Luciola cruciata (LcL), Hotaria parvura (HpL), and Luciola mingrelica (LmL). Among these, PmL, PpL, and LcL showed the expected thioesterification activities toward both substrates. All the enzymes exhibited (R)-enantioselectivity toward ketoprofen, which had same tendency as firefly luciferase from Luciola lateralis (LUC-H). HpL and LmL, however, did not accept ketoprofen, although they had thioesterification activity toward C12. These results indicate that the substrate acceptance of luciferases for the thioesterification reaction varies dramatically relying on the origin of firefly. Hence we focused primarily on PmL and investigated the effect of pH on enzymatic activity. In addition, by determining the kinetic parameters at various pH values, we verified that the kcat parameter contributed to the preferential enantioselectivity of this enzyme.