IDENTIFICATION OF THE N-TERMINAL DOMAIN OF ENZYME-I OF THE ESCHERICHIA-COLI PHOSPHOENOLPYRUVATE-SUGAR PHOSPHOTRANSFERASE SYSTEM PRODUCED BY PROTEOLYTIC DIGESTION

被引：30

作者：

LEE, BR ^{[1
]}

LECCHI, P ^{[1
]}

PANNELL, L ^{[1
]}

JAFFE, H ^{[1
]}

PETERKOFSKY, A ^{[1
]}

机构：

[1] NIH,BETHESDA,MD 20892

来源：

ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS | 1994年 / 312卷 / 01期

关键词：

D O I：

10.1006/abbi.1994.1289

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：

The phosphoenolpyruvate:sugar phosphotransferase system of bacteria plays an important role in the concomitant uptake and phosphorylation of numerous sugars. The first protein in the pathway of phosphotransfer of the phosphoenolpyruvate:sugar phosphotransferase system is Enzyme I. It has been shown that a stable N-terminal domain can be produced by treatment of the purified protein with various proteolytic enzymes. We show here that the region from glutamate-252 to leucine-264 is accessible to proteolysis resulting in N-terminal cores ranging from M(r) 27521 to 28799. (C) 1994 Academic Press, Inc.

引用

页码：121 / 124

页数：4

共 11 条

[1] A COMPREHENSIVE SET OF SEQUENCE-ANALYSIS PROGRAMS FOR THE VAX [J].