4l9y: Difference between revisions
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{{STRUCTURE_4l9y| PDB=4l9y | SCENE= }} | |||
===Crystal Structure of Rhodobacter sphaeroides malyl-CoA lyase in complex with magnesium, glyoxylate, and propionyl-CoA=== | |||
{{ABSTRACT_PUBMED_24206647}} | |||
==Function== | |||
[[http://www.uniprot.org/uniprot/MCAL_RHOS4 MCAL_RHOS4]] Catalyzes the reversible condensation of glyoxylate and acetyl-CoA to L-malyl-CoA and the reversible condensation of glyoxylate and propionyl-CoA to beta-methylmalyl-CoA.<ref>PMID:20047909</ref> | |||
==About this Structure== | |||
[[4l9y]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4L9Y OCA]. | |||
==Reference== | |||
<ref group="xtra">PMID:024206647</ref><references group="xtra"/><references/> | |||
[[Category: Malyl-CoA lyase]] | |||
[[Category: Kerfeld, C A.]] | |||
[[Category: Zarzycki, J.]] | |||
[[Category: Lyase]] | |||
[[Category: Tim barrel]] | |||
Revision as of 07:18, 4 December 2013
Crystal Structure of Rhodobacter sphaeroides malyl-CoA lyase in complex with magnesium, glyoxylate, and propionyl-CoA
Template:ABSTRACT PUBMED 24206647
Function
[MCAL_RHOS4] Catalyzes the reversible condensation of glyoxylate and acetyl-CoA to L-malyl-CoA and the reversible condensation of glyoxylate and propionyl-CoA to beta-methylmalyl-CoA.[1]
About this Structure
4l9y is a 6 chain structure. Full crystallographic information is available from OCA.
Reference
- Zarzycki J, Kerfeld CA. The crystal structures of the tri-functional Chloroflexus aurantiacus and bi-functional Rhodobacter sphaeroides malyl-CoA lyases and comparison with CitE-like superfamily enzymes and malate synthases. BMC Struct Biol. 2013 Nov 9;13(1):28. PMID:24206647 doi:https://dx.doi.org/10.1186/1472-6807-13-28
- ↑ Erb TJ, Frerichs-Revermann L, Fuchs G, Alber BE. The apparent malate synthase activity of Rhodobacter sphaeroides is due to two paralogous enzymes, (3S)-Malyl-coenzyme A (CoA)/{beta}-methylmalyl-CoA lyase and (3S)- Malyl-CoA thioesterase. J Bacteriol. 2010 Mar;192(5):1249-58. doi: 10.1128/JB.01267-09. Epub 2010 Jan 4. PMID:20047909 doi:https://dx.doi.org/10.1128/JB.01267-09
