Effect of phosphorylation on the reaction rate of unnatural electrophiles with 2-keto-3-deoxy-6-phosphogluconate aldolase

被引：10

作者：

Cotterill, IC ^{[1
]}

Shelton, MC ^{[1
]}

Machemer, DEW ^{[1
]}

Henderson, DP ^{[1
]}

Toone, EJ ^{[1
]}

机构：

[1] Duke Univ, Dept Chem, Durham, NC 27708 USA

来源：

JOURNAL OF THE CHEMICAL SOCIETY-PERKIN TRANSACTIONS 1 | 1998年 / 07期

关键词：

D O I：

10.1039/a706764j

中图分类号：

O62 [有机化学];

学科分类号：

070303 ; 081704 ;

摘要：

D-Glyceraldehyde is accepted as an electrophile by 2-keto-3-deoxy-6-phosphogluconate (KDPG) aldolase (EC 4.1.2.14) at 1% the rate of natural substrate, D-glyceraldehyde 3-phosphate. Accordingly, it was expected that addition of a phosphate moiety at C3 or C4 of unnatural aldehydes would enhance their activity as electrophilic substrates. Furthermore, phosphate would act as a useful protecting group during synthetic manipulations of the aldol adduct. A variety of phosphorylated and non-phosphorylated aldehydes were synthesized and evaluated as substrates for KDPG aldolase. Although small variations in reaction rate were observed, phosphorylation failed to provide a universal rate enhancement. Evaluation of substrate kinetic parameters revealed that the high rate of reaction of D-glyceraldehyde 3-phosphate compared to related electrophiles is entirely due to the efficiency of turnover with little change in binding exhibited among various substrates.

引用

页码：1335 / 1341

页数：7

共 42 条

[21] NEW SYNTHETIC APPLICATIONS OF SIALIC-ACID ALDOLASE, A USEFUL CATALYST FOR KDO SYNTHESIS - RELATION BETWEEN SUBSTRATE CONFORMATION AND ENZYME STEREOSELECTIVITY [J].