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. 1967 Nov;105(2):467–472. doi: 10.1042/bj1050467

Studies on the enzymic degradation of L-serine O-sulphate by a rat liver preparation

J H Thomas 1, N Tudball 1
PMCID: PMC1198333  PMID: 5583990

Abstract

1. The enzyme system of rat liver responsible for the degradation of l-serine O-sulphate was purified 300-fold and the optimum conditions for the activity were determined. 2. Inorganic sulphate, pyruvate and ammonia were found to be the products of enzyme action on lserine O-sulphate, being formed in equivalent amounts under all conditions examined. No free l-serine was detected as a product of enzyme action. 3. The enzyme preparation was free from other serine-metabolizing systems such as O-phospho-l-serine phosphatase and l-serine dehydratase. 4. The enzyme has a very narrow substrate specificity and is inactive towards a wide variety of related sulphate esters and amino acids. 5. Pyridoxal 5′-phosphate is capable of catalysing the non-enzymic breakdown of l-serine O-sulphate in the presence of metal salts to yield inorganic sulphate, pyruvate and ammonia as products. 6. The possible role of pyridoxal 5′-phosphate as a coenzyme in the enzymic degradation of l-serine O-sulphate is discussed.

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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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