Arg169 is essential for catalytic activity of 3-hydroxybenzoate 6-hydroxylase from Klebsiella pneumoniae M5a1

D Q Liu, H Liu, X L Gao, D J Leak, N Y Zhou

Research output: Contribution to journalArticle

13 Citations (Scopus)

Abstract

3-Hydroxybenzoate 6-hydroxylase from Klebsiella pneumoniae M5a1 is an enzyme that utilizes 3-hydroxybenzoate (3-HBA) as substrate yielding gentisate. Site-directed mutagenesis was carried out to define which residues may be involved in catalytic reaction. Substitution of arginine to glutamate at position 169 of the enzyme resulted in the complete loss of catalytic activity. This indicated Arg169 may play an important role in 3-HBA 6-hydroxylase catalysis.
Original languageEnglish
Pages (from-to)53-59
Number of pages7
JournalMicrobiological Research
Volume160
Issue number1
DOIs
Publication statusPublished - 28 Feb 2005

Fingerprint

Klebsiella pneumoniae
arginine glutamate
Gentisates
Hydroxybenzoates
Enzymes
Site-Directed Mutagenesis
Catalysis
3-hydroxybenzoate-6-hydroxylase

Cite this

Arg169 is essential for catalytic activity of 3-hydroxybenzoate 6-hydroxylase from Klebsiella pneumoniae M5a1. / Liu, D Q; Liu, H; Gao, X L; Leak, D J; Zhou, N Y.

In: Microbiological Research, Vol. 160, No. 1, 28.02.2005, p. 53-59.

Research output: Contribution to journalArticle

@article{1436bf5e83194207bb286360b929fd80,
title = "Arg169 is essential for catalytic activity of 3-hydroxybenzoate 6-hydroxylase from Klebsiella pneumoniae M5a1",
abstract = "3-Hydroxybenzoate 6-hydroxylase from Klebsiella pneumoniae M5a1 is an enzyme that utilizes 3-hydroxybenzoate (3-HBA) as substrate yielding gentisate. Site-directed mutagenesis was carried out to define which residues may be involved in catalytic reaction. Substitution of arginine to glutamate at position 169 of the enzyme resulted in the complete loss of catalytic activity. This indicated Arg169 may play an important role in 3-HBA 6-hydroxylase catalysis.",
author = "Liu, {D Q} and H Liu and Gao, {X L} and Leak, {D J} and Zhou, {N Y}",
year = "2005",
month = "2",
day = "28",
doi = "10.1016/j.micres.2004.09.003",
language = "English",
volume = "160",
pages = "53--59",
journal = "Microbiological Research",
issn = "0944-5013",
publisher = "Urban und Fischer Verlag Jena",
number = "1",

}

TY - JOUR

T1 - Arg169 is essential for catalytic activity of 3-hydroxybenzoate 6-hydroxylase from Klebsiella pneumoniae M5a1

AU - Liu, D Q

AU - Liu, H

AU - Gao, X L

AU - Leak, D J

AU - Zhou, N Y

PY - 2005/2/28

Y1 - 2005/2/28

N2 - 3-Hydroxybenzoate 6-hydroxylase from Klebsiella pneumoniae M5a1 is an enzyme that utilizes 3-hydroxybenzoate (3-HBA) as substrate yielding gentisate. Site-directed mutagenesis was carried out to define which residues may be involved in catalytic reaction. Substitution of arginine to glutamate at position 169 of the enzyme resulted in the complete loss of catalytic activity. This indicated Arg169 may play an important role in 3-HBA 6-hydroxylase catalysis.

AB - 3-Hydroxybenzoate 6-hydroxylase from Klebsiella pneumoniae M5a1 is an enzyme that utilizes 3-hydroxybenzoate (3-HBA) as substrate yielding gentisate. Site-directed mutagenesis was carried out to define which residues may be involved in catalytic reaction. Substitution of arginine to glutamate at position 169 of the enzyme resulted in the complete loss of catalytic activity. This indicated Arg169 may play an important role in 3-HBA 6-hydroxylase catalysis.

UR - http://dx.doi.org/10.1016/j.micres.2004.09.003

U2 - 10.1016/j.micres.2004.09.003

DO - 10.1016/j.micres.2004.09.003

M3 - Article

VL - 160

SP - 53

EP - 59

JO - Microbiological Research

JF - Microbiological Research

SN - 0944-5013

IS - 1

ER -