The phosphate recognition site of Escherichia coli maltodextrin phosphorylase.

Abstract:

:The role of two positively charged amino acid residues located at the active site of Escherichia coli maltodextrin phosphorylase was investigated by site-directed mutagenesis. Substitution of Lys539 by an arginine caused a 600-fold reduction, substitution of Arg534 by a glutamine caused an even larger 7000-fold reduction of the catalytic rate while substrate binding remained essentially unaffected. Since the Arg534----Gln exchange reduces the catalytic rate near to inactivity and even the conservative Lys534----Arg exchange caused a marked decrease of activity, the central functional role of both positively charged residues in phosphorylase catalysis anticipated by the crystallographic analysis of the corresponding amino acid residues Arg569 and Lys574 in the catalytic site of phosphorylase b was confirmed.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Schinzel R,Drueckes P

doi

10.1016/0014-5793(91)80956-4

subject

Has Abstract

pub_date

1991-07-29 00:00:00

pages

125-8

issue

1-2

eissn

0014-5793

issn

1873-3468

pii

0014-5793(91)80956-4

journal_volume

286

pub_type

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