|
type |
Journal Article |
authors |
Farrington, G. K.; Kumar, A.; Shames, S. L.; Ewaskiewicz, J. I.; Ash, D. E.; Wedler, F. C. |
title |
Threonine synthase of Escherichia coli: inhibition by classical and slow-binding analogues of homoserine phosphate |
journal |
Arch Biochem Biophys |
Activity |
4.2.3.1 |
ui |
94058249 |
year |
(1993) |
volume |
307 |
number |
1 |
pages |
165-74. |
| |
keywords |
2-Amino-5-phosphonovalerate/analogs & derivatives/pharmacology |
abstract |
L-threo-3-Hydroxyhomoserine phosphate, derived from the antimetabolites L-threo-3-hydroxyaspartate and L-threo-3-hydroxyhomoserine [Shames, S. L., Ash, D. E., Wedler, F. C., and Villafranca, J. J. (1984) J. Biol. Chem. 258, 15331-15339], is a classical competitive inhibitor of threonine synthase (Ki = 6 microM) with structural elements of both substrate and product. L-2-Amino-5-phosphonovaleric acid also inhibits the enzyme competitively with a Ki (31 microM), comparable to Km for L- homoserine phosphate. In contrast, a structural analogue of Hse-P, L-2- amino-3-[(phosphonomethyl)thio]propionic acid exhibits a Ki = 0.11 microM (ca. 100-fold less than Km for L-Hse-P), along with "slow |
last changed |
2002/11/12 16:17 |
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