A structural mapping of mutations causing succinyl-CoA:3-ketoacid CoA transferase (SCOT) deficiency

A structural mapping of mutations causing succinyl-CoA:3-ketoacid CoA transferase (SCOT) deficiency

Succinyl-CoA:3-ketoacid CoA transferase (SCOT) deficiency is a rare inherited metabolic disorder of ketone metabolism, characterized by ketoacidotic episodes and often permanent ketosis. To date there are ∼20 disease-associated alleles on the OXCT1 gene that encodes the mitochondrial enzyme SCOT. SC...

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Main Authors: Shafqat, Naeem, Kavanagh, Kate L., Sass, Jörn Oliver, Christensen, Ernst, Fukao, Toshiyuki, Lee, Wen Hwa, Oppermann, Udo, Yue, Wyatt W.
Format: Online
Language:English
Published: Springer Netherlands 2013
Online Access:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3825524/
id pubmed-3825524
recordtype oai_dc
spelling pubmed-38255242013-11-21 A structural mapping of mutations causing succinyl-CoA:3-ketoacid CoA transferase (SCOT) deficiency Shafqat, Naeem Kavanagh, Kate L. Sass, Jörn Oliver Christensen, Ernst Fukao, Toshiyuki Lee, Wen Hwa Oppermann, Udo Yue, Wyatt W. Original Article Succinyl-CoA:3-ketoacid CoA transferase (SCOT) deficiency is a rare inherited metabolic disorder of ketone metabolism, characterized by ketoacidotic episodes and often permanent ketosis. To date there are ∼20 disease-associated alleles on the OXCT1 gene that encodes the mitochondrial enzyme SCOT. SCOT catalyzes the first, rate-limiting step of ketone body utilization in peripheral tissues, by transferring a CoA moiety from succinyl-CoA to form acetoacetyl-CoA, for entry into the tricarboxylic acid cycle for energy production. We have determined the crystal structure of human SCOT, providing a molecular understanding of the reported mutations based on their potential structural effects. An interactive version of this manuscript (which may contain additional mutations appended after acceptance of this manuscript) may be found on the web address: http://www.thesgc.org/jimd/SCOT. Springer Netherlands 2013-02-19 2013 /pmc/articles/PMC3825524/ /pubmed/23420214 http://dx.doi.org/10.1007/s10545-013-9589-z Text en © The Author(s) 2013 Open AccessThis article is distributed under the terms of the Creative Commons Attribution License which permits any use, distribution, and reproduction in any medium, provided the original author(s) and the source are credited.
repository_type Open Access Journal
institution_category Foreign Institution
institution US National Center for Biotechnology Information
building NCBI PubMed
collection Online Access
language English
format Online
author Shafqat, Naeem
Kavanagh, Kate L.
Sass, Jörn Oliver
Christensen, Ernst
Fukao, Toshiyuki
Lee, Wen Hwa
Oppermann, Udo
Yue, Wyatt W.
spellingShingle Shafqat, Naeem
Kavanagh, Kate L.
Sass, Jörn Oliver
Christensen, Ernst
Fukao, Toshiyuki
Lee, Wen Hwa
Oppermann, Udo
Yue, Wyatt W.
A structural mapping of mutations causing succinyl-CoA:3-ketoacid CoA transferase (SCOT) deficiency
author_facet Shafqat, Naeem
Kavanagh, Kate L.
Sass, Jörn Oliver
Christensen, Ernst
Fukao, Toshiyuki
Lee, Wen Hwa
Oppermann, Udo
Yue, Wyatt W.
author_sort Shafqat, Naeem
title A structural mapping of mutations causing succinyl-CoA:3-ketoacid CoA transferase (SCOT) deficiency
title_short A structural mapping of mutations causing succinyl-CoA:3-ketoacid CoA transferase (SCOT) deficiency
title_full A structural mapping of mutations causing succinyl-CoA:3-ketoacid CoA transferase (SCOT) deficiency
title_fullStr A structural mapping of mutations causing succinyl-CoA:3-ketoacid CoA transferase (SCOT) deficiency
title_full_unstemmed A structural mapping of mutations causing succinyl-CoA:3-ketoacid CoA transferase (SCOT) deficiency
title_sort structural mapping of mutations causing succinyl-coa:3-ketoacid coa transferase (scot) deficiency
description Succinyl-CoA:3-ketoacid CoA transferase (SCOT) deficiency is a rare inherited metabolic disorder of ketone metabolism, characterized by ketoacidotic episodes and often permanent ketosis. To date there are ∼20 disease-associated alleles on the OXCT1 gene that encodes the mitochondrial enzyme SCOT. SCOT catalyzes the first, rate-limiting step of ketone body utilization in peripheral tissues, by transferring a CoA moiety from succinyl-CoA to form acetoacetyl-CoA, for entry into the tricarboxylic acid cycle for energy production. We have determined the crystal structure of human SCOT, providing a molecular understanding of the reported mutations based on their potential structural effects. An interactive version of this manuscript (which may contain additional mutations appended after acceptance of this manuscript) may be found on the web address: http://www.thesgc.org/jimd/SCOT.
publisher Springer Netherlands
publishDate 2013
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3825524/
_version_ 1612025962172514304

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