3zht: Difference between revisions
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{{STRUCTURE_3zht| PDB=3zht | SCENE= }} | |||
===Crystal structure of the SucA domain of Mycobacterium smegmatis KGD, first post-decarboxylation intermediate from 2-oxoadipate=== | |||
{{ABSTRACT_PUBMED_24171907}} | |||
The | ==Function== | ||
[[http://www.uniprot.org/uniprot/KGD_MYCS2 KGD_MYCS2]] Shows three enzymatic activities that share a first common step, the attack of thiamine-PP on 2-oxoglutarate (alpha-ketoglutarate, KG), leading to the formation of an enamine-thiamine-PP intermediate upon decarboxylation. Thus, displays KGD activity, catalyzing the decarboxylation from five-carbon 2-oxoglutarate to four-carbon succinate semialdehyde (SSA). Also catalyzes C-C bond formation between the activated aldehyde formed after decarboxylation of alpha-ketoglutarate and the carbonyl of glyoxylate (GLX), to yield 2-hydroxy-3-oxoadipate (HOA), which spontaneously decarboxylates to form 5-hydroxylevulinate (HLA). And is also a component of the 2-oxoglutarate dehydrogenase (ODH) complex, that catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). The KG decarboxylase and KG dehydrogenase reactions provide two alternative, tightly regulated, pathways connecting the oxidative and reductive branches of the TCA cycle.<ref>PMID:19019160</ref> <ref>PMID:21867916</ref> | |||
==About this Structure== | |||
[[3zht]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZHT OCA]. | |||
==Reference== | |||
<ref group="xtra">PMID:024171907</ref><references group="xtra"/><references/> | |||
[[Category: Alzari, P M.]] | |||
[[Category: Barilone, N.]] | |||
[[Category: Bellinzoni, M.]] | |||
[[Category: Wagner, T.]] | |||
[[Category: E1o]] | |||
[[Category: Oxidoreductase]] | |||
