PDB rendering based on 3had.
PDB Ortholog search:
List of PDB id codes
, 1F0Y , 1F12 , 1F14 , 1F17 , 1IL0 , 1LSJ , 1LSO , 1M75 , 1M76 , 2HDH , 3HAD 3RQS
HADH (; HAD; HADH1; HADHSC; HCDH; HHF4; MSCHAD; SCHAD)
OMIM: 601609 MGI: 96009 HomoloGene: 55888 GeneCards: HADH Gene
108.91 – 108.96 Mb
131.23 – 131.27 Mb
Hydroxyacyl-Coenzyme A dehydrogenase also known as HADH is an enzyme which in humans is encoded by the HADH gene. [1 ] [2 ]
Function [ edit ]
This gene 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. [3 ]
Clinical significance [ edit ]
Mutations in this gene cause one form of familial
hyperinsulinemic hypoglycemia. A deficiency is associated with [4 ] 3-hydroxyacyl-coenzyme A dehydrogenase deficiency.
See also [ edit ]
References [ edit ]
^ Craig I, Tolley E, Bobrow M (1976). "A preliminary analysis of the segregation of human hydroxyacyl coenzyme A dehydrogenase in human-mouse somatic cell hybrids". Cytogenet. Cell Genet. 16 (1–5): 114–7. doi: 10.1159/000130568. PMID 975867.
^ Yang SY, He XY, Schulz H (October 2005). "3-Hydroxyacyl-CoA dehydrogenase and short chain 3-hydroxyacyl-CoA dehydrogenase in human health and disease". FEBS J. 272 (19): 4874–83. doi: 10.1111/j.1742-4658.2005.04911.x. PMID 16176262.
^ "Entrez Gene: HADH".
^ Molven A, Matre GE, Duran M, Wanders RJ, Rishaug U, Njølstad PR, Jellum E, Søvik O (January 2004). "Familial hyperinsulinemic hypoglycemia caused by a defect in the SCHAD enzyme of mitochondrial fatty acid oxidation". Diabetes 53 (1): 221–7. doi: 10.2337/diabetes.53.1.221. PMID 14693719.
External links [ edit ]
This article incorporates text from the United States National Library of Medicine, which is in the public domain.
3had: BIOCHEMICAL CHARACTERIZATION AND STRUCTURE DETERMINATION OF HUMAN HEART SHORT CHAIN L-3-HYDROXYACYL COA DEHYDROGENASE PROVIDE INSIGHT INTO CATALYTIC MECHANISM
1m75: Crystal Structure of the N208S Mutant of L-3-Hydroxyacyl-COA Dehydrogenase in Complex with NAD and Acetoacetyl-COA
2hdh: BIOCHEMICAL CHARACTERIZATION AND STRUCTURE DETERMINATION OF HUMAN HEART SHORT CHAIN L-3-HYDROXYACYL COA DEHYDROGENASE PROVIDE INSIGHT INTO CATALYTIC MECHANISM
1lsj: Crystal Structure of the E110Q Mutant of L-3-Hydroxyacyl-CoA Dehydrogenase in Complex with NAD
1f0y: L-3-HYDROXYACYL-COA DEHYDROGENASE COMPLEXED WITH ACETOACETYL-COA AND NAD+
1f14: L-3-HYDROXYACYL-COA DEHYDROGENASE (APO)
1m76: Crystal Structure of the S137C Mutant of L-3-HYDROXYACYL-COA Dehydrogenase in Complex with NAD and Acetoacetyl-COA
1lso: Crystal Structure of the S137A mutant of L-3-Hydroxyacyl-CoA Dehydrogenase in Complex with NAD
3hdh: PIG HEART SHORT CHAIN L-3-HYDROXYACYL COA DEHYDROGENASE REVISITED: SEQUENCE ANALYSIS AND CRYSTAL STRUCTURE DETERMINATION
1f12: L-3-HYDROXYACYL-COA DEHYDROGENASE COMPLEXED WITH 3-HYDROXYBUTYRYL-COA
1f17: L-3-HYDROXYACYL-COA DEHYDROGENASE COMPLEXED WITH NADH
1il0: X-RAY CRYSTAL STRUCTURE OF THE E170Q MUTANT OF HUMAN L-3-HYDROXYACYL-COA DEHYDROGENASE