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http://purl.uniprot.org/citations/18492492http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18492492http://www.w3.org/2000/01/rdf-schema#comment"In addition to the main transaminase reaction, the pyridoxal 5'-phosphate-dependent enzyme human liver peroxisomal alanine:glyoxylate aminotransferase (AGT) is able to catalyze the alpha,beta-elimination of beta-chloro-L-alanine with a catalytic efficiency similar to that of the physiological transaminase reaction with L-alanine. On the other hand, during the reaction of AGT with L-cysteine, changes in the coenzyme forms and analysis of the products reveal the occurrence of both beta-elimination and half-transamination of L-cysteine together with the pyruvate transamination. A mechanism in which a ketimine species is the common intermediate of half-transamination and beta-elimination of L-cysteine is proposed. L-cysteine partitions between these two reactions with a ratio of approximately 2.5. Rapid scanning stopped-flow and quench flow experiments permit the identification of reaction intermediates and the measurements of the kinetic parameters of L-cysteine half-transamination. The k(cat) of this reaction is 200- or 60-fold lower than that of L-alanine and L-serine, respectively. Conversely, L-cysteine binds to AGT with a binding affinity 30- and 200-fold higher than that of L-alanine and L-serine, respectively. This appears to be consistent with the calculated interaction energies of the L-cysteine, L-alanine and L-serine docked at the active site of AGT."xsd:string
http://purl.uniprot.org/citations/18492492http://purl.org/dc/terms/identifier"doi:10.1016/j.bbapap.2008.04.013"xsd:string
http://purl.uniprot.org/citations/18492492http://purl.uniprot.org/core/author"Paiardini A."xsd:string
http://purl.uniprot.org/citations/18492492http://purl.uniprot.org/core/author"Borri Voltattorni C."xsd:string
http://purl.uniprot.org/citations/18492492http://purl.uniprot.org/core/author"Cellini B."xsd:string
http://purl.uniprot.org/citations/18492492http://purl.uniprot.org/core/author"Montioli R."xsd:string
http://purl.uniprot.org/citations/18492492http://purl.uniprot.org/core/author"Bertoldi M."xsd:string
http://purl.uniprot.org/citations/18492492http://purl.uniprot.org/core/date"2008"xsd:gYear
http://purl.uniprot.org/citations/18492492http://purl.uniprot.org/core/name"Biochim Biophys Acta"xsd:string
http://purl.uniprot.org/citations/18492492http://purl.uniprot.org/core/pages"1356-1362"xsd:string
http://purl.uniprot.org/citations/18492492http://purl.uniprot.org/core/title"Reactions of human liver peroxisomal alanine:glyoxylate aminotransferase with beta-chloro-L-alanine and L-cysteine: spectroscopic and kinetic analysis."xsd:string
http://purl.uniprot.org/citations/18492492http://purl.uniprot.org/core/volume"1784"xsd:string
http://purl.uniprot.org/citations/18492492http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/18492492
http://purl.uniprot.org/citations/18492492http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/18492492
http://purl.uniprot.org/uniprot/P21549#attribution-18808F6096265E952FA3506DD68000F2http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/18492492
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http://purl.uniprot.org/uniprot/#_P21549-mappedCitation-18492492http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/18492492
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http://purl.uniprot.org/uniprot/#_Q16171-mappedCitation-18492492http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/18492492
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