IDENTIFICATION OF RESIDUES INVOLVED IN THE BINDING OF METHIONINE BY ESCHERICHIA-COLI METHIONYL-TRANSFER-RNA SYNTHETASE

被引：27

作者：

FOURMY, D ^{[1
]}

MECHULAM, Y ^{[1
]}

BRUNIE, S ^{[1
]}

BLANQUET, S ^{[1
]}

FAYAT, G ^{[1
]}

机构：

[1] ECOLE POLYTECH,CNRS,BIOCHIM LAB,URA 240,F-91128 PALAISEAU,FRANCE

来源：

FEBS LETTERS | 1991年 / 292卷 / 1-2期

关键词：

METHIONYL-TRANSFER-RNA SYNTHETASE; METHIONINE; SPECTROPHOTOFLUORIMETRY;

D O I：

10.1016/0014-5793(91)80879-8

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Comparison of the amino-acid sequences of several methionyl-tRNA synthetases indicates the occurrence of a few conserved motifs, having a possible functional significance. The role of one of these motifs, centered at position 300 in the E. coli enzyme sequence, was assayed by the use of site-directed mutagenesis. Substitution of the His301 or Trp305 residues by Ala resulted in a large decrease in methionine affinity, whereas the change of Val298 into Ala had only a moderate effect. The catalytic rate of the enzyme was unimpaired by these substitutions. It is concluded that the above conserved amino-acid region is located at or close to the amino-acid binding pocket of methionyl-tRNA synthetase.

引用

页码：259 / 263

页数：5

共 21 条

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