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Title 

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

Authors 

Joong Su KimSuk Hoon KohHyun Jae ShinDae Sil LeeSe Young Lee

Publisher 

Portland Press

Issue Date 

1999

Citation 

Biotechnology and Applied Biochemistry, vol. 29, no. 0, pp. 11-17

Keywords 

bacterial enzymefructose 1 phosphategalactose 1 phosphate uridylyltransferaseglucose 1 phosphateuridine triphosphate glucose 1 phosphate uridylyltransferaseaffinity chromatographyamino acid sequenceamino terminal sequenceenzyme activitygel filtration chromatography

Abstract 

An extremely thermostable UDP-GlcNAc pyrophosphorylase has been purified from Thermus caldophilus GK24 by chromatographic methods including ionexchange, 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°C and its half-life at 95°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 I-phosphate, a precursor of UDP-GlcNAc. The enzyme showed a broad substrate specificity with sugar I-phosphates, including glucose I-phosphate, GlcNAc-1-P and xylose I-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.

ISSN 

0885-4513

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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