Hydroxyacyl Coenzyme A Dehydrogenase (HADH)

HADHSC; HADH1; SCHAD; L-3-Hydroxyacyl-Coenzyme A Dehydrogenase,Short Chain; Medium and short-chain L-3-hydroxyacyl-coenzyme A dehydrogenase

SPN	T102
HGNC	4799
MGI	96009
PubMed	21252247
RGD	69321
UniProt	Q16836
Wiki	HADH

HADH is a member of the 3-hydroxyacyl-CoA dehydrogenase gene family. The encoded protein functions in the mitochondrial matrix to catalyze the oxidation of straight-chain 3-hydroxyacyl-CoAs as part of the beta-oxidation pathway. Its enzymatic activity is highest with medium-chain-length fatty acids. Mutations in this gene cause one form of familial hyperinsulinemic hypoglycemia. The human genome contains a related pseudogene.Human HADH encodes a deduced 314-amino acid protein composed of a 12-residue mitochondrial import signal peptide and a 302-residue mature HADH protein with a calculated molecular mass of 34.3 kD. The sequence of the mature protein shows 94% identity with HADH from pig heart. Northern blot analysis revealed expression of HADH in liver, kidney, pancreas, heart, and skeletal muscle.

Reference

"Human short-chain L-3-hydroxyacyl-CoA dehydrogenase: cloning and characterization of the coding sequence."
Biochem. Biophys. Res. Commun. 223:718-723(1996) [PubMed] [Europe PMC] [Abstract]

"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]

"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]

"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]

"Initial characterization of the human central proteome."
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]

"An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]

"Biochemical characterization and crystal structure determination of human heart short chain L-3-hydroxyacyl-CoA dehydrogenase provide insights into catalytic mechanism."
Biochemistry 38:5786-5798(1999) [PubMed] [Europe PMC] [Abstract]

"Sequestration of the active site by interdomain shifting. Crystallographic and spectroscopic evidence for distinct conformations of L-3-hydroxyacyl-CoA dehydrogenase."
J. Biol. Chem. 275:27186-27196(2000) [PubMed] [Europe PMC] [Abstract]

"3-hydroxyacyl-CoA dehydrogenase and short chain 3-hydroxyacyl-CoA dehydrogenase in human health and disease."
FEBS J. 272:4874-4883(2005) [PubMed] [Europe PMC] [Abstract]

"Fulminant hepatic failure associated with mutations in the medium and short chain L-3-hydroxyacyl-CoA dehydrogenase gene."
J. Inherit. Metab. Dis. 23 Suppl. 1:127-127(2000)

"Hyperinsulinism in short-chain L-3-hydroxyacyl-CoA dehydrogenase deficiency reveals the importance of beta-oxidation in insulin secretion."
J. Clin. Invest. 108:457-465(2001) [PubMed] [Europe PMC] [Abstract]