<HashMap><database>biostudies-other</database><scores/><additional><omics_type>Unknown</omics_type><volume>110(4)</volume><submitter>Thomas JH</submitter><journal>The Biochemical journal</journal><pagination>687-92</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC1187441</full_dataset_link><abstract>1. l-Serine O-sulphate and l-threonine O-sulphate are degraded in the presence of pyridoxal 5'-phosphate to yield equimolar amounts of the corresponding keto acid, ammonia and sulphate. 2. Pyridoxal catalyses the same reactions at a faster rate. 3. One of a number of bi- or ter-valent metal ions must be present for these degradations to proceed. The reaction rates are dependent on a number of factors including pH and the nature of the metal ion used. 4. Studies with related sulphate esters indicate that the alpha-hydrogen atom and the amino group are essential for activity. 5. Spectral changes during the pyridoxal and pyridoxal 5'-phosphate catalysis of l-serine O-sulphate breakdown suggest the formation of a Schiff base. 6. The mechanism for these reactions appears to be in accordance with the general mechanism proposed for pyridoxal-catalysed alphabeta-elimination reactions.</abstract><repository>biostudies-other</repository><data_source>Europe PMC</data_source><pubmed_authors>Tudball N</pubmed_authors><pubmed_authors>Thomas JH</pubmed_authors><pubmed_authors>Dodgson KS</pubmed_authors></additional><is_claimable>false</is_claimable><name>The pyridoxal- and pyridoxal 5'-phosphate-catalysed non-enzymic degradations of l-serine o-sulphate and related compounds.</name><description>1. l-Serine O-sulphate and l-threonine O-sulphate are degraded in the presence of pyridoxal 5'-phosphate to yield equimolar amounts of the corresponding keto acid, ammonia and sulphate. 2. Pyridoxal catalyses the same reactions at a faster rate. 3. One of a number of bi- or ter-valent metal ions must be present for these degradations to proceed. The reaction rates are dependent on a number of factors including pH and the nature of the metal ion used. 4. Studies with related sulphate esters indicate that the alpha-hydrogen atom and the amino group are essential for activity. 5. Spectral changes during the pyridoxal and pyridoxal 5'-phosphate catalysis of l-serine O-sulphate breakdown suggest the formation of a Schiff base. 6. The mechanism for these reactions appears to be in accordance with the general mechanism proposed for pyridoxal-catalysed alphabeta-elimination reactions.</description><dates><release>1968-01-01T00:00:00Z</release><publication>1968 Dec</publication><modification>2019-08-04T08:08:16Z</modification><creation>2019-08-04T08:08:16Z</creation></dates><accession>S-EPMC1187441</accession><cross_references><DOI>10.1042/bj1100687 </DOI></cross_references></HashMap>