| Literature DB >> 14646194 |
Cuddapah Suresh1, Motomitsu Kitaoka, Kiyoshi Hayashi.
Abstract
A putative alpha-glucosidase belonging to glycosyl hydrolase family 4 of Thermotoga maritima (TM0752) was expressed in Escherichia coli and it was found that the recombinant protein (Agu4B) was a p-nitrophenyl alpha-D-glucuronopyranoside hydrolyzing alpha-glucuronidase, not alpha-glucosidase. It did not hydrolyze 4-O-methyl-D-glucuronoxylan or its fragment oligosaccharides. Agu4B was thermostable with an optimum temperature of 80 degrees C. It strictly required Mn(2+) and thiol compounds for its activity. The presence of NAD(+) slightly activated the enzyme. The amino acid sequence of Agu4B showed higher identity with Agu4A (another alpha-glucuronidase of T. maritima, 61%) than with AglA (alpha-glucosidase of T. maritima, 48%).Entities:
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Year: 2003 PMID： 14646194 DOI： 10.1271/bbb.67.2359
Source DB: PubMed Journal: Biosci Biotechnol Biochem ISSN： 0916-8451 Impact factor: 2.043