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Hinman MB, Villemez CL. Glucomannan Biosynthesis Catalyzed by Pisum sativum Enzymes. Plant Physiol. 1975;56(5):608-12doi: 10.1104/pp.56.5.608.
Hinman, M. B., & Villemez, C. L. (1975). Glucomannan Biosynthesis Catalyzed by Pisum sativum Enzymes. Plant physiology, 56(5), 608-12. https://doi.org/10.1104/pp.56.5.608
Hinman, M B, and Villemez, C L. "Glucomannan Biosynthesis Catalyzed by Pisum sativum Enzymes." Plant physiology vol. 56,5 (1975): 608-12. doi: https://doi.org/10.1104/pp.56.5.608
Hinman MB, Villemez CL. Glucomannan Biosynthesis Catalyzed by Pisum sativum Enzymes. Plant Physiol. 1975 Nov;56(5):608-12. doi: 10.1104/pp.56.5.608. PMID: 16659354; PMCID: PMC541881.
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Plant Physiol. 1975 Nov;56(5):608-12. doi: 10.1104/pp.56.5.608.

Glucomannan Biosynthesis Catalyzed by Pisum sativum Enzymes.

Plant physiology

M B Hinman, C L Villemez

Affiliations

  1. Division of Biochemistry and Department of Chemistry, University of Wyoming, Laramie, Wyoming 82071.

PMID: 16659354 PMCID: PMC541881 DOI: 10.1104/pp.56.5.608

Abstract

The results of molecular weight studies, structural analysis of the [(14)C]polysaccharides, and enzymic properties indicate that the Pisum sativum guanosine diphosphosphate glucose: glucosyltransferase is an enzymic component involved in the biosynthesis of glucomannan chains. The properties of the Pisum sativum particulate enzyme are essentially identical to the glucomannan synthetase obtained from Phaseolus aureus. Also present in the particulate preparation is an enzyme which catalyzes the formation of a [(14)C]mannolipid, using guanosine diphosphate-[(14)C]mannose as a substrate. The [(14)C]mannolipid is hydrolyzed by treatment with 0.012 m HCl, but is stable to treatment with 0.09 m NaOH. The formation of the [(14)C]mannolipid is apparently reversed by guanosine diphosphate, but not by guanosine monophosphate. The chromatographic mobility of the [(14)C]mannolipid is identical to that of a similar mannolipid synthesized by a Phaseolus aureus enzyme.

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