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B6db references: 94058249

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
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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