1zy8: Difference between revisions
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===The crystal structure of dihydrolipoamide dehydrogenase and dihydrolipoamide dehydrogenase-binding protein (didomain) subcomplex of human pyruvate dehydrogenase complex.=== | ===The crystal structure of dihydrolipoamide dehydrogenase and dihydrolipoamide dehydrogenase-binding protein (didomain) subcomplex of human pyruvate dehydrogenase complex.=== | ||
{{ABSTRACT_PUBMED_16263718}} | {{ABSTRACT_PUBMED_16263718}} | ||
==Disease== | |||
[[http://www.uniprot.org/uniprot/DLDH_HUMAN DLDH_HUMAN]] Note=Defects in DLD are involved in the development of congenital infantile lactic acidosis. Defects in DLD are a cause of maple syrup urine disease (MSUD) [MIM:[http://omim.org/entry/248600 248600]]. MSUD is characterized by mental and physical retardation, feeding problems and a maple syrup odor to the urine. The keto acids of the branched-chain amino acids are present in the urine, resulting from a block in oxidative decarboxylation. [[http://www.uniprot.org/uniprot/ODPX_HUMAN ODPX_HUMAN]] Defects in PDHX are the cause of pyruvate dehydrogenase E3-binding protein deficiency (PDHXD) [MIM:[http://omim.org/entry/245349 245349]].<ref>PMID:9399911</ref> | |||
==Function== | |||
[[http://www.uniprot.org/uniprot/DLDH_HUMAN DLDH_HUMAN]] Lipoamide dehydrogenase is a component of the glycine cleavage system as well as of the alpha-ketoacid dehydrogenase complexes. Involved in the hyperactivation of spermatazoa during capacitation and in the spermatazoal acrosome reaction. [[http://www.uniprot.org/uniprot/ODPX_HUMAN ODPX_HUMAN]] Required for anchoring dihydrolipoamide dehydrogenase (E3) to the dihydrolipoamide transacetylase (E2) core of the pyruvate dehydrogenase complexes of eukaryotes. This specific binding is essential for a functional PDH complex. | |||
==About this Structure== | ==About this Structure== | ||
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==Reference== | ==Reference== | ||
<ref group="xtra">PMID:016263718</ref><references group="xtra"/> | <ref group="xtra">PMID:016263718</ref><references group="xtra"/><references/> | ||
[[Category: Dihydrolipoyl dehydrogenase]] | [[Category: Dihydrolipoyl dehydrogenase]] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
Revision as of 03:06, 25 March 2013
The crystal structure of dihydrolipoamide dehydrogenase and dihydrolipoamide dehydrogenase-binding protein (didomain) subcomplex of human pyruvate dehydrogenase complex.
Template:ABSTRACT PUBMED 16263718
Disease
[DLDH_HUMAN] Note=Defects in DLD are involved in the development of congenital infantile lactic acidosis. Defects in DLD are a cause of maple syrup urine disease (MSUD) [MIM:248600]. MSUD is characterized by mental and physical retardation, feeding problems and a maple syrup odor to the urine. The keto acids of the branched-chain amino acids are present in the urine, resulting from a block in oxidative decarboxylation. [ODPX_HUMAN] Defects in PDHX are the cause of pyruvate dehydrogenase E3-binding protein deficiency (PDHXD) [MIM:245349].[1]
Function
[DLDH_HUMAN] Lipoamide dehydrogenase is a component of the glycine cleavage system as well as of the alpha-ketoacid dehydrogenase complexes. Involved in the hyperactivation of spermatazoa during capacitation and in the spermatazoal acrosome reaction. [ODPX_HUMAN] Required for anchoring dihydrolipoamide dehydrogenase (E3) to the dihydrolipoamide transacetylase (E2) core of the pyruvate dehydrogenase complexes of eukaryotes. This specific binding is essential for a functional PDH complex.
About this Structure
1zy8 is a 15 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.
See Also
Reference
- Ciszak EM, Makal A, Hong YS, Vettaikkorumakankauv AK, Korotchkina LG, Patel MS. How dihydrolipoamide dehydrogenase-binding protein binds dihydrolipoamide dehydrogenase in the human pyruvate dehydrogenase complex. J Biol Chem. 2006 Jan 6;281(1):648-55. Epub 2005 Nov 1. PMID:16263718 doi:10.1074/jbc.M507850200
- ↑ Aral B, Benelli C, Ait-Ghezala G, Amessou M, Fouque F, Maunoury C, Creau N, Kamoun P, Marsac C. Mutations in PDX1, the human lipoyl-containing component X of the pyruvate dehydrogenase-complex gene on chromosome 11p1, in congenital lactic acidosis. Am J Hum Genet. 1997 Dec;61(6):1318-26. PMID:9399911 doi:S0002-9297(07)60233-X
Proteopedia Page Contributors and Editors (what is this?)
- Dihydrolipoyl dehydrogenase
- Homo sapiens
- Ciszak, E M.
- Hong, Y S.
- Korotchkina, L G.
- Makal, A.
- Patel, M S.
- Vettaikkorumakankauv, A K.
- Alpha-keto acid complex
- Dihydrolipoamide dehydrogenase
- Dihydrolipoamide dehydrogenase binding protein
- E3
- E3-binding protein
- Flavin adenine dinucleotide cofactor
- Human
- Oxidoreductase
- Pyruvate dehydrogenase complex
