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- W2034218100 endingPage "1973" @default.
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- W2034218100 abstract "The presence of a stable allantoinase in Lathyrus sativas and its de novo synthesis at a maximal rate in the first 48 hr of germination have been demonstrated. The plumule and radicle together exhibited highest enzyme activity. L. sativas allantoinase has been purified nearly 35-fold. The purified enzyme was optically active around pH 7.5, did not require any metal ion for activity and exhibited a Km of 2·56 mM for (±)-allantoin, and an activation energy of 5·6 kcal/mol. Unlike other plant allantoinases, the L. sativus enzyme is highly specific for (±)-allantoin and is shown to be a sulfhydryl enzyme which apparently exists in a stable form in vivo obviating the need for added sulfhydryl compounds for maximal activity." @default.
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- W2034218100 date "1975-09-01" @default.
- W2034218100 modified "2023-09-27" @default.
- W2034218100 title "The allantoinase of Lathyrus sativus" @default.
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- W2034218100 doi "https://doi.org/10.1016/0031-9422(75)83107-4" @default.
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