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. 1968 Jan;43(1):103–112. doi: 10.1104/pp.43.1.103

Phosphorylases I and II of Maize Endosperm 1,2,3

C Y Tsai a, O E Nelson a
PMCID: PMC396019  PMID: 16656726

Abstract

Two phosphorylases have been found in the endosperm of Zea mays. Phosphorylase I is found through all stages of endosperm development and seed germination investigated. The other enzyme, phosphorylase II appears only at the stage of rapid starch biosynthesis and is not found during germination. At 22 days after pollination, the activity of phosphorylase II is 10 times that of phosphorylase I. These 2 phosphorylases are separable by column chromatography and behave differently in several respects.

Phosphorylase I cannot utilize maltose as a primer while phosphorylase II does so readily. Furthermore, phosphorylase II can synthesize an amylose-like polymer from a “primer free” system after a lag phase.

Phosphorylase II is inhibited severely at pH 5.8 by ATP, GTP, ADP, and GDP, and less drastically by UTP, CTP, UDP and CDP. Phosphorylase I is somewhat inhibited by purine nucleotides but not by pyrimidine nucleotides. In all cases, the inhibition is pH-dependent. Phosphorylase I is inhibited competitively by ATP while phosphorylase II is inhibited non-competitively.

Phosphorylase II is markedly stimulated by 10 mm Mg2+ and by 2 mm ethylenediamine tetraacetic acid while phosphorylase I is relatively little affected.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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