3iqd
From Proteopedia
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===Structure of Octopine-dehydrogenase in complex with NADH and Agmatine=== | ===Structure of Octopine-dehydrogenase in complex with NADH and Agmatine=== | ||
| + | {{ABSTRACT_PUBMED_20808820}} | ||
| - | + | ==Function== | |
| - | + | [[http://www.uniprot.org/uniprot/Q9BHM6_PECMA Q9BHM6_PECMA]] Catalyzes the reverse reaction of octopine dehydrogenation. Acts on L-arginine in preference to other substrates such as canavanine, cysteine, L-alanine, ornithine or norvaline, owing to the presence of the positively charged guanidium group.<ref>PMID:18028427</ref><ref>PMID:18599075</ref> | |
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==About this Structure== | ==About this Structure== | ||
| - | + | [[3iqd]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Pecten_maximus Pecten maximus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3IQD OCA]. | |
==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID: | + | <ref group="xtra">PMID:020808820</ref><references group="xtra"/><references/> |
[[Category: D-octopine dehydrogenase]] | [[Category: D-octopine dehydrogenase]] | ||
[[Category: Pecten maximus]] | [[Category: Pecten maximus]] | ||
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[[Category: Octopine]] | [[Category: Octopine]] | ||
[[Category: Oxidoreductase]] | [[Category: Oxidoreductase]] | ||
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Revision as of 09:39, 27 March 2013
Contents |
Structure of Octopine-dehydrogenase in complex with NADH and Agmatine
Template:ABSTRACT PUBMED 20808820
Function
[Q9BHM6_PECMA] Catalyzes the reverse reaction of octopine dehydrogenation. Acts on L-arginine in preference to other substrates such as canavanine, cysteine, L-alanine, ornithine or norvaline, owing to the presence of the positively charged guanidium group.[1][2]
About this Structure
3iqd is a 1 chain structure with sequence from Pecten maximus. Full crystallographic information is available from OCA.
Reference
- Smits SH, Meyer T, Mueller A, van Os N, Stoldt M, Willbold D, Schmitt L, Grieshaber MK. Insights into the mechanism of ligand binding to octopine dehydrogenase from Pecten maximus by NMR and crystallography. PLoS One. 2010 Aug 19;5(8):e12312. PMID:20808820 doi:10.1371/journal.pone.0012312
- ↑ Muller A, Janssen F, Grieshaber MK. Putative reaction mechanism of heterologously expressed octopine dehydrogenase from the great scallop, Pecten maximus (L). FEBS J. 2007 Dec;274(24):6329-39. Epub 2007 Nov 19. PMID:18028427 doi:EJB6151
- ↑ Smits SH, Mueller A, Schmitt L, Grieshaber MK. A structural basis for substrate selectivity and stereoselectivity in octopine dehydrogenase from Pecten maximus. J Mol Biol. 2008 Aug 1;381(1):200-11. Epub 2008 Jun 7. PMID:18599075 doi:10.1016/j.jmb.2008.06.003
