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- W86174137 abstract "ABSTRACT. There are two primary forms of the enzymes of the pentose phosphate pathway in Candida utilis, a yeast that can grow on pentoses as well as on hexoses. Trans-aldolase, one of the enzymes in this pathway, has an additional form which is a hybrid formed by exchange of subunits of the other two isozymes. There are no differences in the kinetic properties of these isozymes; their only difference lies in their structure, indicating different genetic origin as shown by the sequence of a peptide from the active site of transaldolase I and III. In this peptide, substitution of a tyrosine residue by a histidine residue is observed. Even though there are two identical chains in isozymes I or III, a single active site can be detected. The participation of a lysine and a histidine and the role of a neighboring cysteine in the mechanism of action of the enzyme are discussed." @default.
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- W86174137 date "1975-01-01" @default.
- W86174137 modified "2023-10-05" @default.
- W86174137 title "ISOZYMES OF THE PENTOSE PHOSPHATE PATHWAY" @default.
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- W86174137 doi "https://doi.org/10.1016/b978-0-12-472701-4.50052-8" @default.
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