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2005 | 52 | 2 | 527-534
Article title

Some structural properties of plant serine:glyoxylate aminotransferase?

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EN
Abstracts
EN
The structural properties of photorespiratory serine:glyoxylate aminotransferases (SGAT, EC 2.6.1.45) from maize (Zea mays L.) and wheat (Triticum aestivum L.) leaves were examined. By means of molecular sieving on Zorbax SE-250 column and filtration through centrifugal filters it was shown that dimers of wheat enzyme (molecular mass of about 90 kDa) dissociate into component monomers (molecular mass of about 45 kDa) upon decrease in pH value (from 9.1 or 7.0 to 6.5). At pH 9.1 a 50-fold decrease of ionic strength elicited a similar effect. Under the same conditions homodimers of the maize enzyme (molecular mass similar to that of the wheat enzyme) remained stable. Immunoblot analysis with polyclonal antiserum against wheat seedling SGAT on leaf homogenates or highly purified preparations of both enzymes showed that the immunogenic portions of the wheat enzyme are divergent from those of the maize enzyme. The sequence of 136 amino acids of the maize enzyme and 78 amino acids of the wheat enzyme was established by tandem mass spectrometry with time of flight analyzer. The two enzymes likely share similarity in tertiary and quaternary structures as well as high level of hydrophobicity on their molecular surfaces. They likely differ in the mechanism of transport from the site of biosynthesis to peroxisomes as well as in some aspects of secondary structure.
Publisher

Year
Volume
52
Issue
2
Pages
527-534
Physical description
Dates
published
2005
received
2004-11-18
revised
2005-02-11
accepted
2005-03-13
(unknown)
2005-06-06
Contributors
  • Department of Biochemistry, Faculty of Agriculture and Biology, Warsaw Agricultural University, Warszawa, Poland
  • Department of Biochemistry, Faculty of Agriculture and Biology, Warsaw Agricultural University, Warszawa, Poland
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Document Type
Publication order reference
Identifiers
YADDA identifier
bwmeta1.element.bwnjournal-article-abpv52i2p527kz
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