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Enzymic synthesis of indole-3-acetyl-1-O-beta-d-glucose. I. Partial purification and characterization of the enzyme from Zea maysThe first enzyme-catalyzed reaction leading from indole-3-acetic acid (IAA) to the myo-inositol esters of IAA is the synthesis of indole-3-acetyl-1-O-beta-D-glucose from uridine-5'-diphosphoglucose (UDPG) and IAA. The reaction is catalyzed by the enzyme, UDPG-indol-3-ylacetyl glucosyl transferase (IAA-glucose-synthase). This work reports methods for the assay of the enzyme and for the extraction and partial purification of the enzyme from kernels of Zea mays sweet corn. The enzyme has an apparent molecular weight of 46,500 an isoelectric point of 5.5, and its pH optimum lies between 7.3 and 7.6. The enzyme is stable to storage at zero degrees but loses activity during column chromatographic procedures which can be restored only fractionally by addition of column eluates. The data suggest either multiple unknown cofactors or conformational changes leading to activity loss.
Document ID
20040112094
Acquisition Source
Ames Research Center
Document Type
Reprint (Version printed in journal)
Authors
Leznicki, A. J.
(Michigan State University East Lansing 48824-1312, United States)
Bandurski, R. S.
Date Acquired
August 21, 2013
Publication Date
January 1, 1988
Publication Information
Publication: Plant physiology
Volume: 88
ISSN: 0032-0889
Subject Category
Life Sciences (General)
Funding Number(s)
CONTRACT_GRANT: NAGW-97
CONTRACT_GRANT: DMB-8504231
CONTRACT_GRANT: NAG2-362
Distribution Limits
Public
Copyright
Other
Keywords
NASA Discipline Number 40-10
Non-NASA Center
NASA Discipline Plant Biology
NASA Program Space Biology

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