Purification and Characterization of N-Acetylglucosamine-6-phosphate Deacetylase from a Psychrotrophic Marine Bacterium, Alteromonas Species

A psychrotrophic bacterium, strain Mct-9, which produced an N-acetylglucosamine-6-phosphate deacetylase, was isolated from a deep-seawater sample in the Mariana Trough. The Mct-9 strain was identified as Alteromonas sp. The native enzyme had a molecular mass of 164,000 Da, and was predicted to be co...

Full description

Saved in:
Bibliographic Details
Published in:Marine biotechnology (New York, N.Y.) N.Y.), 2000-01, Vol.2 (1), p.57-64
Main Authors: Yamano, N, Higashida, N, Endo, C, Sakata, N, Fujishima, S, Maruyama, A, Higashihara, T
Format: Article
Language:English
Subjects:
Alteromonas
Bacteria
Chemical analysis
Enzymes
Marine
Molecular weight
N-Acetylglucosamine
N-Acetylglucosamine-6-phosphate
N-acetylglucosamine-6-phosphate deacetylase
Phosphate
Phosphates
Psychrophiles
psychrotrophic microorganisms
Purification
Seawater
Sulfates
Temperature
Vibrio cholerae
Water analysis
Water purification
Waterborne diseases
Citations: Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:A psychrotrophic bacterium, strain Mct-9, which produced an N-acetylglucosamine-6-phosphate deacetylase, was isolated from a deep-seawater sample in the Mariana Trough. The Mct-9 strain was identified as Alteromonas sp. The native enzyme had a molecular mass of 164,000 Da, and was predicted to be composed of four identical subunits with molecular masses of 41,000 Da. The purified enzyme hydrolyzed N-acetylglucosamine (GlcNAc), GlcNAc-6-phosphate, and GlcNAc-6-sulfate. Considering the low K(m) and high k(cat)/K(m) for GlcNAc-6-phosphate, it probably acts as a GlcNAc-6-phosphate deacetylase in vivo. The enzyme was functional in the temperature range of 5 degrees to 70 degrees C and displayed optimal activity at 55 degrees C. The optimal temperature was higher than that of the deacetylase from the mesophilic bacterium Vibrio cholerae non-O1. The characteristics of the GlcNAc-6-phosphate deacetylase from Alteromonas sp. are unique among psychrotrophs and psychrophiles, whose intracellular enzymes are mostly thermolabile.
ISSN:1436-2228
1436-2236
DOI:10.1007/s101269900008