2bfc: Difference between revisions
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[[Image:2bfc.png|left|200px]] | [[Image:2bfc.png|left|200px]] | ||
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==About this Structure== | ==About this Structure== | ||
[[2bfc]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BFC OCA]. | |||
==Reference== | ==Reference== | ||
<ref group="xtra">PMID:16472748</ref><references group="xtra"/> | <ref group="xtra">PMID:16472748</ref><ref group="xtra">PMID:15166214</ref><ref group="xtra">PMID:12902323</ref><ref group="xtra">PMID:11069910</ref><references group="xtra"/> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Brautigam, C A.]] | [[Category: Brautigam, C A.]] | ||
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[[Category: Tomchick, D R.]] | [[Category: Tomchick, D R.]] | ||
[[Category: Wynn, R M.]] | [[Category: Wynn, R M.]] | ||
[[Category: Conformational switch | [[Category: Acylation]] | ||
[[Category: | [[Category: Branched-chain]] | ||
[[Category: Conformational switch]] | |||
[[Category: Ketoacid dehydrogenase]] | |||
[[Category: Maple syrup urine disease]] | |||
[[Category: Multi- enzyme complex]] | |||
[[Category: Oxidative decarboxylation]] | |||
[[Category: Oxidoreductase]] | |||
[[Category: Phosphorylation]] | |||
[[Category: Reactivity]] | |||
[[Category: Thiamine diphosphate]] |
Revision as of 03:14, 15 March 2011
REACTIVITY MODULATION OF HUMAN BRANCHED-CHAIN ALPHA-KETOACID DEHYDROGENASE BY AN INTERNAL MOLECULAR SWITCHREACTIVITY MODULATION OF HUMAN BRANCHED-CHAIN ALPHA-KETOACID DEHYDROGENASE BY AN INTERNAL MOLECULAR SWITCH
Template:ABSTRACT PUBMED 16472748
About this StructureAbout this Structure
2bfc is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
[xtra 1][xtra 2][xtra 3][xtra 4]
- ↑ Machius M, Wynn RM, Chuang JL, Li J, Kluger R, Yu D, Tomchick DR, Brautigam CA, Chuang DT. A versatile conformational switch regulates reactivity in human branched-chain alpha-ketoacid dehydrogenase. Structure. 2006 Feb;14(2):287-98. PMID:16472748 doi:10.1016/j.str.2005.10.009
- ↑ Li J, Wynn RM, Machius M, Chuang JL, Karthikeyan S, Tomchick DR, Chuang DT. Cross-talk between thiamin diphosphate binding and phosphorylation loop conformation in human branched-chain alpha-keto acid decarboxylase/dehydrogenase. J Biol Chem. 2004 Jul 30;279(31):32968-78. Epub 2004 May 27. PMID:15166214 doi:http://dx.doi.org/10.1074/jbc.M403611200
- ↑ Wynn RM, Machius M, Chuang JL, Li J, Tomchick DR, Chuang DT. Roles of His291-alpha and His146-beta' in the reductive acylation reaction catalyzed by human branched-chain alpha-ketoacid dehydrogenase: refined phosphorylation loop structure in the active site. J Biol Chem. 2003 Oct 31;278(44):43402-10. Epub 2003 Aug 5. PMID:12902323 doi:http://dx.doi.org/10.1074/jbc.M306204200
- ↑ Wynn RM, Ho R, Chuang JL, Chuang DT. Roles of active site and novel K+ ion-binding site residues in human mitochondrial branched-chain alpha-ketoacid decarboxylase/dehydrogenase. J Biol Chem. 2001 Feb 9;276(6):4168-74. Epub 2000 Nov 7. PMID:11069910 doi:10.1074/jbc.M008038200
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OCACategories:
- Pages with broken file links
- Homo sapiens
- Brautigam, C A.
- Chuang, D T.
- Chuang, J L.
- Machius, M.
- Tomchick, D R.
- Wynn, R M.
- Acylation
- Branched-chain
- Conformational switch
- Ketoacid dehydrogenase
- Maple syrup urine disease
- Multi- enzyme complex
- Oxidative decarboxylation
- Oxidoreductase
- Phosphorylation
- Reactivity
- Thiamine diphosphate