4adc: Difference between revisions
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4adc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4adc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4adc RCSB], [http://www.ebi.ac.uk/pdbsum/4adc PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4adc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4adc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4adc RCSB], [http://www.ebi.ac.uk/pdbsum/4adc PDBsum]</span></td></tr> | ||
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== Function == | |||
[[http://www.uniprot.org/uniprot/ASTC_ECOLI ASTC_ECOLI]] Catalyzes the transamination of N(2)-succinylornithine and alpha-ketoglutarate into N(2)-succinylglutamate semialdehyde and glutamate. Can also act as an acetylornithine aminotransferase.<ref>PMID:9696779</ref> | |||
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== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Revision as of 20:59, 25 December 2014
Structural and functional study of succinyl-ornithine transaminase from E. coliStructural and functional study of succinyl-ornithine transaminase from E. coli
Structural highlights
Function[ASTC_ECOLI] Catalyzes the transamination of N(2)-succinylornithine and alpha-ketoglutarate into N(2)-succinylglutamate semialdehyde and glutamate. Can also act as an acetylornithine aminotransferase.[1] Publication Abstract from PubMedpossesses two acyl ornithine aminotransferases, one catabolic (AstC) and the other anabolic (ArgD), that participate in L-arginine metabolism. Although only 58% identical, the enzymes have been shown to be functionally interchangeable. Here we have purified AstC and have obtained X-ray crystal structures of apo and holo-AstC and of the enzyme complexed with its physiological substrate, succinylornithine. We compare the structures obtained in this study with those of ArgD from obtained elsewhere, finding several notable differences. Docking studies were used to explore the docking modes of several substrates (ornithine, succinylornithine and acetylornithine) and the co-substrate glutamate/alpha-ketogluterate. The docking studies support our observations that AstC has a strong preference for acylated ornithine species over ornithine itself, and suggest that the increase in specificity associated with acylation is caused by steric and desolvation effects rather than specific interactions between the substrate and enzyme. Determination of the Structure of the Catabolic N-Succinylornithine Transaminase (AstC) from Escherichia coli.,Newman J, Seabrook S, Surjadi R, Williams CC, Lucent D, Wilding M, Scott C, Peat TS PLoS One. 2013;8(3):e58298. doi: 10.1371/journal.pone.0058298. Epub 2013 Mar 6. PMID:23484010[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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