Type |
Details |
Score |
Genotype |
Symbol: |
Acox1/Acox1 |
Background: |
involves: 129P2/OlaHsd * C57BL/6J |
Zygosity: |
hm |
Has Mutant Allele: |
true |
|
•
•
•
•
•
|
DO Term |
|
•
•
•
•
•
|
Allele |
Name: |
enoyl-Coenzyme A, hydratase/3-hydroxyacyl Coenzyme A dehydrogenase; targeted mutation 1, Janardan K Reddy |
Allele Type: |
Targeted |
Attribute String: |
Null/knockout |
|
•
•
•
•
•
|
Publication |
First Author: |
Dirkx R |
Year: |
2007 |
Journal: |
Biochem Biophys Res Commun |
Title: |
Beta-oxidation in hepatocyte cultures from mice with peroxisomal gene knockouts. |
Volume: |
357 |
Issue: |
3 |
Pages: |
718-23 |
|
•
•
•
•
•
|
Publication |
First Author: |
Ding J |
Year: |
2013 |
Journal: |
Cell Rep |
Title: |
The peroxisomal enzyme L-PBE is required to prevent the dietary toxicity of medium-chain fatty acids. |
Volume: |
5 |
Issue: |
1 |
Pages: |
248-58 |
|
•
•
•
•
•
|
Publication |
First Author: |
Qi C |
Year: |
1999 |
Journal: |
J Biol Chem |
Title: |
Absence of spontaneous peroxisome proliferation in enoyl-CoA Hydratase/L-3-hydroxyacyl-CoA dehydrogenase-deficient mouse liver. Further support for the role of fatty acyl CoA oxidase in PPARalpha ligand metabolism. |
Volume: |
274 |
Issue: |
22 |
Pages: |
15775-80 |
|
•
•
•
•
•
|
Publication |
First Author: |
Baes M |
Year: |
2002 |
Journal: |
J Neuropathol Exp Neurol |
Title: |
The neuronal migration defect in mice with Zellweger syndrome (Pex5 knockout) is not caused by the inactivity of peroxisomal beta-oxidation. |
Volume: |
61 |
Issue: |
4 |
Pages: |
368-74 |
|
•
•
•
•
•
|
Publication |
First Author: |
Ranea-Robles P |
Year: |
2021 |
Journal: |
Kidney360 |
Title: |
Peroxisomal L-bifunctional protein (EHHADH) deficiency causes male-specific kidney hypertrophy and proximal tubular injury in mice. |
Volume: |
2 |
Issue: |
9 |
Pages: |
1441-1454 |
|
•
•
•
•
•
|
Publication |
First Author: |
Houten SM |
Year: |
2012 |
Journal: |
J Lipid Res |
Title: |
Peroxisomal L-bifunctional enzyme (Ehhadh) is essential for the production of medium-chain dicarboxylic acids. |
Volume: |
53 |
Issue: |
7 |
Pages: |
1296-303 |
|
•
•
•
•
•
|
Publication |
First Author: |
Autio KJ |
Year: |
2014 |
Journal: |
Biochem J |
Title: |
Role of AMACR (α-methylacyl-CoA racemase) and MFE-1 (peroxisomal multifunctional enzyme-1) in bile acid synthesis in mice. |
Volume: |
461 |
Issue: |
1 |
Pages: |
125-35 |
|
•
•
•
•
•
|
Publication |
First Author: |
Violante S |
Year: |
2019 |
Journal: |
FASEB J |
Title: |
Peroxisomes can oxidize medium- and long-chain fatty acids through a pathway involving ABCD3 and HSD17B4. |
Volume: |
33 |
Issue: |
3 |
Pages: |
4355-4364 |
|
•
•
•
•
•
|
Publication |
First Author: |
Jia Y |
Year: |
2003 |
Journal: |
J Biol Chem |
Title: |
Overexpression of peroxisome proliferator-activated receptor-alpha (PPARalpha)-regulated genes in liver in the absence of peroxisome proliferation in mice deficient in both L- and D-forms of enoyl-CoA hydratase/dehydrogenase enzymes of peroxisomal beta-oxidation system. |
Volume: |
278 |
Issue: |
47 |
Pages: |
47232-9 |
|
•
•
•
•
•
|
Publication |
First Author: |
Ferdinandusse S |
Year: |
2005 |
Journal: |
J Biol Chem |
Title: |
Developmental changes of bile acid composition and conjugation in L- and D-bifunctional protein single and double knockout mice. |
Volume: |
280 |
Issue: |
19 |
Pages: |
18658-66 |
|
•
•
•
•
•
|
Genotype |
Symbol: |
Ehhadh/Ehhadh Hsd17b4/Hsd17b4 |
Background: |
involves: 129P2/OlaHsd * 129S1/Sv * 129X1/SvJ * C57BL/6J |
Zygosity: |
cx |
Has Mutant Allele: |
true |
|
•
•
•
•
•
|
Genotype |
Symbol: |
Ehhadh/Ehhadh |
Background: |
involves: 129P2/OlaHsd * C57BL/6J |
Zygosity: |
hm |
Has Mutant Allele: |
true |
|
•
•
•
•
•
|
Publication |
First Author: |
Hayashi H |
Year: |
1998 |
Journal: |
J Biol Chem |
Title: |
Molecular characterization of a glyoxysomal long chain acyl-CoA oxidase that is synthesized as a precursor of higher molecular mass in pumpkin. |
Volume: |
273 |
Issue: |
14 |
Pages: |
8301-7 |
|
•
•
•
•
•
|
Publication |
First Author: |
Pedersen L |
Year: |
2005 |
Journal: |
J Mol Biol |
Title: |
Acyl-CoA oxidase 1 from Arabidopsis thaliana. Structure of a key enzyme in plant lipid metabolism. |
Volume: |
345 |
Issue: |
3 |
Pages: |
487-500 |
|
•
•
•
•
•
|
Publication |
First Author: |
Nakade Y |
Year: |
2017 |
Journal: |
PLoS One |
Title: |
Conophylline inhibits non-alcoholic steatohepatitis in mice. |
Volume: |
12 |
Issue: |
6 |
Pages: |
e0178436 |
|
•
•
•
•
•
|
Publication |
First Author: |
Arguin G |
Year: |
2017 |
Journal: |
Sci Rep |
Title: |
The loss of P2X7 receptor expression leads to increase intestinal glucose transit and hepatic steatosis. |
Volume: |
7 |
Issue: |
1 |
Pages: |
12917 |
|
•
•
•
•
•
|
Publication |
First Author: |
Yoo HS |
Year: |
2015 |
Journal: |
J Toxicol Environ Health A |
Title: |
Comparative analysis of the relationship between trichloroethylene metabolism and tissue-specific toxicity among inbred mouse strains: liver effects. |
Volume: |
78 |
Issue: |
1 |
Pages: |
15-31 |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
83
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Domain |
Description: |
Acyl-CoA oxidase (ACO) acts on CoA derivatives of fatty acids with chain lengths from 8 to 18. It catalyses the first and rate-determining step of the peroxisomal beta-oxidation of fatty acids [].Acyl-CoA oxidase is a homodimer and the polypeptide chain of the subunit is folded into the N-terminal alpha-domain, beta-domain, and C-terminal alpha-domain []. Functional differences between the peroxisomal acyl-CoA oxidases and the mitochondrial acyl-CoA dehydrogenases are attributed to structural differences in the FAD environments []. Experimental data indicate that, in the pumpkin, the expression patternof ACOX is very similar to that of the glyoxysomal enzyme 3-ketoacyl-CoA thiolase []. In humans, defects in ACOX1 are the cause of pseudoneonatal adrenoleukodystrophy, also known as peroxisomal acyl-CoA oxidase deficiency. Pseudo-NALD is a peroxisomal single-enzyme disorder. Clinical features include mental retardation, leukodystrophy, seizures, mild hepatomegaly and hearing deficit. Pseudo-NALD is characterised by increased plasma levels of very-long chain fatty acids due to a decrease in, or absence of, peroxisome acyl-CoA oxidase activity, despite the peroxisomes being intact and functioning.This entry represents the Acyl-CoA oxidase C-terminal. |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Family |
Description: |
Acyl-CoA oxidase (ACO) acts on CoA derivatives of fatty acids with chain lengths from 8 to 18. It catalyses the first and rate-determining step of the peroxisomal beta-oxidation of fatty acids and a major producer of hydrogen peroxide (H2O2) [, ].Acyl-CoA oxidase is a homodimer and the polypeptide chain of the subunit is folded into the N-terminal alpha-domain, beta-domain, and C-terminal alpha-domain [, ]. Functional differences between the peroxisomal acyl-CoA oxidases and the mitochondrial acyl-CoA dehydrogenases are attributed to structural differences in the FAD environments []. Experimental data indicate that in the pumpkin, the expression pattern of ACOX is very similar to that of the glyoxysomal enzyme 3-ketoacyl-CoA thiolase []. In humans, defects in ACOX1 are the cause of pseudoneonatal adrenoleukodystrophy, also known as peroxisomal acyl-CoA oxidase deficiency. Clinical features include mental retardation, leukodystrophy, seizures, mild hepatomegaly and hearing deficit. Pseudo-NALD is characterised by increased plasma levels of very-long chain fatty acids due to a decrease in, or absence of, peroxisome acyl-CoA oxidase activity, despite the peroxisomes being intact and functioning []. |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
143
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
700
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
632
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
661
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
681
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
647
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
681
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
625
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
685
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
673
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
697
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Publication |
First Author: |
Nakajima Y |
Year: |
2002 |
Journal: |
J Biochem |
Title: |
Three-dimensional structure of the flavoenzyme acyl-CoA oxidase-II from rat liver, the peroxisomal counterpart of mitochondrial acyl-CoA dehydrogenase. |
Volume: |
131 |
Issue: |
3 |
Pages: |
365-74 |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
201
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
499
 |
Fragment?: |
true |
|
•
•
•
•
•
|