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Novel substrates of a ribose-5-phosphate isomerase from Clostridium thermocellum

Paper ID Volume ID Publish Year Pages File Format Full-Text
24752 43535 2009 7 PDF Available
Title
Novel substrates of a ribose-5-phosphate isomerase from Clostridium thermocellum
Abstract

A substrate specificity study of the recombinant D-ribose-5-phosphate isomerase (RpiB) from Clostridium thermocellum was performed. Among all aldopentoses and aldohexoses, the RpiB enzyme displayed activity with L-talose, D-ribose, D-allose, L-allose, L-ribose, and D-talose in decreasing order. The products released were L-tagatose, D-ribulose, D-psicose, L-psicose, L-ribulose, and D-tagatose, respectively. The enzyme showed specificity for aldose substrates possessing hydroxyl groups oriented in the same direction at the C2, C3, and C4 positions. Molecular modeling of the enzyme suggests that the novel substrate specificity may be explained by substrate interactions with residues Tyr42, His98, and His9, which interact with the hydroxyl groups of C2, C3, and C4, respectively, oriented in the same direction. L-Talose and D-ribulose exhibited the highest activity among the aldoses and ketoses, respectively. Ribose 5-phosphate isomerase catalyzed the conversion of L-talose to L-tagatose with an 89% conversion yield after approximately 90 min, while D-ribulose was converted to D-ribose with a 38% conversion yield.

Keywords
Substrate specificity; Isomerization; Ribose 5-phospate isomerase; Clostridium thermocellum; D-Ribose; L-Talose
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Novel substrates of a ribose-5-phosphate isomerase from Clostridium thermocellum
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Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Biotechnology - Volume 139, Issue 1, 1 January 2009, Pages 26–32
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