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http://purl.uniprot.org/citations/19858196http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/19858196http://www.w3.org/2000/01/rdf-schema#comment"The catabolic pathway for branched-chain amino acids includes deamination followed by oxidative decarboxylation of the deaminated product branched-chain alpha-keto acids, catalyzed by the mitochondrial branched-chain aminotransferase (BCATm) and branched-chain alpha-keto acid dehydrogenase enzyme complex (BCKDC). We found that BCATm binds to the E1 decarboxylase of BCKDC, forming a metabolon that allows channeling of branched-chain alpha-keto acids from BCATm to E1. The protein complex also contains glutamate dehydrogenase (GDH1), 4-nitrophenylphosphatase domain and non-neuronal SNAP25-like protein homolog 1, pyruvate carboxylase, and BCKDC kinase. GDH1 binds to the pyridoxamine 5'-phosphate (PMP) form of BCATm (PMP-BCATm) but not to the pyridoxal 5'-phosphate-BCATm and other metabolon proteins. Leucine activates GDH1, and oxidative deamination of glutamate is increased further by addition of PMP-BCATm. Isoleucine and valine are not allosteric activators of GDH1, but in the presence of 5'-phosphate-BCATm, they convert BCATm to PMP-BCATm, stimulating GDH1 activity. Sensitivity to ADP activation of GDH1 was unaffected by PMP-BCATm; however, addition of a 3 or higher molar ratio of PMP-BCATm to GDH1 protected GDH1 from GTP inhibition by 50%. Kinetic results suggest that GDH1 facilitates regeneration of the form of BCATm that binds to E1 decarboxylase of the BCKDC, promotes metabolon formation, branched-chain amino acid oxidation, and cycling of nitrogen through glutamate."xsd:string
http://purl.uniprot.org/citations/19858196http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m109.048777"xsd:string
http://purl.uniprot.org/citations/19858196http://purl.uniprot.org/core/author"Mobley J.A."xsd:string
http://purl.uniprot.org/citations/19858196http://purl.uniprot.org/core/author"Islam M.M."xsd:string
http://purl.uniprot.org/citations/19858196http://purl.uniprot.org/core/author"Chuang D.T."xsd:string
http://purl.uniprot.org/citations/19858196http://purl.uniprot.org/core/author"Wynn R.M."xsd:string
http://purl.uniprot.org/citations/19858196http://purl.uniprot.org/core/author"Hutson S.M."xsd:string
http://purl.uniprot.org/citations/19858196http://purl.uniprot.org/core/author"Nautiyal M."xsd:string
http://purl.uniprot.org/citations/19858196http://purl.uniprot.org/core/date"2010"xsd:gYear
http://purl.uniprot.org/citations/19858196http://purl.uniprot.org/core/name"J Biol Chem"xsd:string
http://purl.uniprot.org/citations/19858196http://purl.uniprot.org/core/pages"265-276"xsd:string
http://purl.uniprot.org/citations/19858196http://purl.uniprot.org/core/title"Branched-chain amino acid metabolon: interaction of glutamate dehydrogenase with the mitochondrial branched-chain aminotransferase (BCATm)."xsd:string
http://purl.uniprot.org/citations/19858196http://purl.uniprot.org/core/volume"285"xsd:string
http://purl.uniprot.org/citations/19858196http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/19858196
http://purl.uniprot.org/citations/19858196http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/19858196
http://purl.uniprot.org/uniprot/P70478#attribution-66687F9891A241D1EE28B67527028564http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/19858196
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http://purl.uniprot.org/uniprot/#_P70478-mappedCitation-19858196http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/19858196
http://purl.uniprot.org/uniprot/#_A0A8I5ZR24-mappedCitation-19858196http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/19858196
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http://purl.uniprot.org/uniprot/#_Q7TPI5-mappedCitation-19858196http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/19858196