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Purification and characterization of arylmalonate decarboxylase from Achromobacter sp. KU1311

Paper ID Volume ID Publish Year Pages File Format Full-Text
22474 43291 2007 5 PDF Available
Title
Purification and characterization of arylmalonate decarboxylase from Achromobacter sp. KU1311
Abstract

We have isolated, purified and characterized arylmalonate decarboxylase (AMDase; EC 4.1.1.76). This is an unique enzyme that gives optically pure arylpropionates from the corresponding arylmalonates. Recently, we have screened similar enzyme producers from soil samples and succeeded in isolating Achromobacter sp. KU1311. The gene encoding the enzyme was cloned and sequenced. The AMDase gene consists of 720 nucleotides, which specifies a 240 amino acid protein with a relative molecular mass of 24,735. This enzyme was purified and its characteristics were compared with those of the hitherto known enzyme from Alcaligenes bronchisepticus KU1201.

Keywords
Achromobacter sp.; arylmalonate decarboxylase; asymmetric decarboxylation; purification
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Purification and characterization of arylmalonate decarboxylase from Achromobacter sp. KU1311
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Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Bioscience and Bioengineering - Volume 104, Issue 4, October 2007, Pages 263–267
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