Biochemical characterization of a UDP-sugar pyrophosphorylase from Thermus caldophilus GK24.

Abstract:

:An extremely thermostable UDP-GlcNAc pyrophosphorylase has been purified from Thermus caldophilus GK24 by chromatographic methods including ion-exchange, hydrophobic interaction, and affinity chromatographies. The specific activity of the enzyme was enriched 41.8-fold, with a recovery of 2%. The molecular mass of the enzyme was 41 kDa by SDS/PAGE and 45 kDa by gel-filtration chromatography. The activity was maximum at 86 degrees C and its half-life at 95 degrees C was 30 min. Its optimum pH was 6.9 in the presence of Mg2+ ions. A biochemical study showed that UDP-GlcNAc pyrophosphorylase activity could be enhanced by fructose 1-phosphate, a precursor of UDP-GlcNAc. The enzyme showed a broad substrate specificity with sugar 1-phosphates, including glucose 1-phosphate, GlcNAc-1-P and xylose 1-phosphate. The enzyme was therefore named UDP-sugar pyrophosphorylase. The N-terminal and internal peptide sequences were determined and compared with known sequences from various sources. It was found that N-terminal sequence is similar to that of UDP-GlcNAc and UDP-glucose pyrophosphorylases from other bacterial sources.

authors

Kim JS,Koh S,Shin HJ,Lee DS,Lee SY

subject

Has Abstract

pub_date

1999-02-01 00:00:00

pages

11-7

eissn

0885-4513

issn

1470-8744

journal_volume

29 ( Pt 1)

pub_type

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