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Characterization of d-galactosyl-β1→4-l-rhamnose phosphorylase from Opitutus terrae

Paper ID Volume ID Publish Year Pages File Format Full-Text
17648 42686 2010 5 PDF Available
Title
Characterization of d-galactosyl-β1→4-l-rhamnose phosphorylase from Opitutus terrae
Abstract

We characterized a glycoside hydrolase family 112 protein from Opitutus terrae (Oter_1377 protein). The enzyme phosphorolyzed d-galactosyl-β1→4-l-rhamnose (GalRha) and also showed phosphorolytic activity on d-galactosyl-β1→3-d-glucose as a minor substrate. In the reverse reaction, the enzyme showed higher activity on l-rhamnose derivatives than on d-glucose derivatives. The enzyme was stable up to 45 °C and at pH 6.0–7.0. The values of kcat and Km of the phosphorolytic activity of the enzyme on GalRha were 60 s−1 and 2.1 mM, respectively. Thus, Oter_1377 protein was identified as d-galactosyl-β1→4-l-rhamnose phosphorylase (GalRhaP). The presence of GalRhaP in O. terrae suggests that genes encoding GalRhaP are widely distributed in different organisms.

Keywords
Glycoside hydrolase family 112; d-Galactosyl-β1→4-l-rhamnose phosphorylase; Phosphorylase; β-Galactoside; Opitutus terrae
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Characterization of d-galactosyl-β1→4-l-rhamnose phosphorylase from Opitutus terrae
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Publisher
Database: Elsevier - ScienceDirect
Journal: Enzyme and Microbial Technology - Volume 46, Issues 3–4, 5 March 2010, Pages 315–319
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
Online Support
Any Questions? feel free to contact us