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Search results 301 to 323 out of 323 for Pon3

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Type Details Score
Publication
- | J:144087
     
First Author: Mouse Genome Informatics Scientific Curators
Year: 2009
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Genome 430 2.0 Array Platform
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Publication
14695884 | J:88273
First Author: Aharoni A
Year: 2004
Journal: Proc Natl Acad Sci U S A
Title: Directed evolution of mammalian paraoxonases PON1 and PON3 for bacterial expression and catalytic specialization.
Volume: 101
Issue: 2
Pages: 482-7
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Allele
Pon3<em1Smoc> | MGI:7291756
Name: paraoxonase 3; endonuclease-mediated mutation 1, Shanghai Model Organisms Center
Allele Type: Endonuclease-mediated
Attribute String: Null/knockout
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Strain
MGI:6476059 | C57BL/6JSmoc-Pon3<em1Smoc>/Smoc
Attribute String: coisogenic, endonuclease-mediated mutation, mutant strain
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Protein Domain
IPR008364 | Paraoxonase2
Type: Family
Description: The serum paraoxonases/arylesterases are enzymes that catalyse the hydrolysisof the toxic metabolites of a variety of organophosphorus insecticides. Theenzymes hydrolyse a broad spectrum of organophosphate substrates, including paraoxon and a number of aromatic carboxylic acid esters (e.g., phenylacetate), and hence confer resistance to organophosphate toxicity []. Mammals have 3 distinct paraoxonase types, termed PON1-3 [, ]. In mice andhumans, the PON genes are found on the same chromosome in close proximity. PON activity has been found in variety of tissues, with highest levels in liver and serum - the source of serum PON is thought to be the liver. Unlike mammals, fish and avian species lack paraoxonase activity. Human and rabbit PONs appear to have two distinct Ca2+ binding sites, onerequired for stability and one required for catalytic activity. The Ca2+dependency of PONs suggests a mechanism of hydrolysis where Ca2+ acts as theelectrophillic catalyst, like that proposed for phospholipase A2. Theparaoxonase enzymes, PON1 and PON3, are high density lipoprotein (HDL)-associated proteins capable of preventing oxidative modification of lowdensity lipoproteins (LPL) []. Although PON2 has oxidative properties, theenzyme does not associate with HDL.Within a given species, PON1, PON2 and PON3 share ~60% amino acid sequence identity, whereas between mammalian species particular PONs (1,2 or 3) share79-90% identity at the amino acid level. Human PON1 and PON3 share numerous conserved phosphorylation and N-glycosylation sites; however, it is not known whether the PON proteins are modified at these sites, or whether modification at these sites is required for activity in vivo [].
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Publication
9032442 | -
 
First Author: Rodrigo L
Year: 1997
Journal: Biochem J
Title: Purification and characterization of paraoxon hydrolase from rat liver.
Volume: 321 ( Pt 3)
Pages: 595-601
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Publication
7749820 | -
First Author: Hegele RA
Year: 1995
Journal: Arterioscler Thromb Vasc Biol
Title: A polymorphism of the paraoxonase gene associated with variation in plasma lipoproteins in a genetic isolate.
Volume: 15
Issue: 1
Pages: 89-95
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Protein Domain
IPR002640 | Arylesterase
Type: Family
Description: The serum paraoxonases/arylesterases are enzymes that catalyse the hydrolysisof the toxic metabolites of a variety of organophosphorus insecticides. Theenzymes hydrolyse a broad spectrum of organophosphate substrates, including paraoxon and a number of aromatic carboxylic acid esters (e.g., phenylacetate), and hence confer resistance to organophosphate toxicity []. Mammals have 3 distinct paraoxonase types, termed PON1-3 [, ]. In mice andhumans, the PON genes are found on the same chromosome in close proximity. PON activity has been found in variety of tissues, with highest levels in liver and serum - the source of serum PON is thought to be the liver. Unlike mammals, fish and avian species lack paraoxonase activity. Human and rabbit PONs appear to have two distinct Ca2+ binding sites, onerequired for stability and one required for catalytic activity. The Ca2+dependency of PONs suggests a mechanism of hydrolysis where Ca2+ acts as theelectrophillic catalyst, like that proposed for phospholipase A2. Theparaoxonase enzymes, PON1 and PON3, are high density lipoprotein (HDL)-associated proteins capable of preventing oxidative modification of lowdensity lipoproteins (LPL) []. Although PON2 has oxidative properties, theenzyme does not associate with HDL.Within a given species, PON1, PON2 and PON3 share ~60% amino acid sequence identity, whereas between mammalian species particular PONs (1,2 or 3) share79-90% identity at the amino acid level. Human PON1 and PON3 share numerous conserved phosphorylation and N-glycosylation sites; however, it is not known whether the PON proteins are modified at these sites, or whether modification at these sites is required for activity in vivo []. This family consists of arylesterases (Also known as serum paraoxonase) . These enzymes hydrolyse organophosphorus esters such as paraoxon and are found in the liver and blood. They confer resistance to organophosphate toxicity []. Human arylesterase (PON1) is associated with HDL and may protect against LDL oxidation [].
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Protein Domain
IPR008363 | Paraoxonase1
Type: Family
Description: The serum paraoxonases/arylesterases are enzymes that catalyse the hydrolysisof the toxic metabolites of a variety of organophosphorus insecticides. Theenzymes hydrolyse a broad spectrum of organophosphate substrates, including paraoxon and a number of aromatic carboxylic acid esters (e.g., phenylacetate), and hence confer resistance to organophosphate toxicity []. Mammals have 3 distinct paraoxonase types, termed PON1-3 [, ]. In mice andhumans, the PON genes are found on the same chromosome in close proximity. PON activity has been found in variety of tissues, with highest levels in liver and serum - the source of serum PON is thought to be the liver. Unlike mammals, fish and avian species lack paraoxonase activity. Human and rabbit PONs appear to have two distinct Ca2+ binding sites, onerequired for stability and one required for catalytic activity. The Ca2+dependency of PONs suggests a mechanism of hydrolysis where Ca2+ acts as theelectrophillic catalyst, like that proposed for phospholipase A2. Theparaoxonase enzymes, PON1 and PON3, are high density lipoprotein (HDL)-associated proteins capable of preventing oxidative modification of lowdensity lipoproteins (LPL) []. Although PON2 has oxidative properties, theenzyme does not associate with HDL.Within a given species, PON1, PON2 and PON3 share ~60% amino acid sequence identity, whereas between mammalian species particular PONs (1,2 or 3) share79-90% identity at the amino acid level. Human PON1 and PON3 share numerous conserved phosphorylation and N-glycosylation sites; however, it is not known whether the PON proteins are modified at these sites, or whether modification at these sites is required for activity in vivo []. Rabbit and human serum PON1 also hydrolyse a variety oflactones and cycliccarbonate esters, including naturally occurring lactones and pharmacologicalagents []. Humans have 2 common PON1 allozymes, determined by the presenceof either arginine or glutamine at position 191. The A-type allozyme (glutamine at position 191) causes low paraoxonase activity []; thispolymorphism is associated with variations in cholesterol and lipoproteinlevels.
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Publication
11038162 | -
First Author: Billecke S
Year: 2000
Journal: Drug Metab Dispos
Title: Human serum paraoxonase (PON1) isozymes Q and R hydrolyze lactones and cyclic carbonate esters.
Volume: 28
Issue: 11
Pages: 1335-42
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Protein
Q8VDG8
Organism: Mus musculus/domesticus
Length: 200  
Fragment?: false
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Protein
Q99JS7
Organism: Mus musculus/domesticus
Length: 108  
Fragment?: false
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Protein
H3BL07
Organism: Mus musculus/domesticus
Length: 135  
Fragment?: true
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Publication
19359600 | J:164769
First Author: She ZG
Year: 2009
Journal: Circ Res
Title: Human paraoxonase gene cluster transgenic overexpression represses atherogenesis and promotes atherosclerotic plaque stability in ApoE-null mice.
Volume: 104
Issue: 10
Pages: 1160-8
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Publication
21354197 | J:178581
First Author: Giordano G
Year: 2011
Journal: Toxicol Appl Pharmacol
Title: Paraoxonase 2 (PON2) in the mouse central nervous system: a neuroprotective role?
Volume: 256
Issue: 3
Pages: 369-78
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Protein
Q62086
Organism: Mus musculus/domesticus
Length: 354  
Fragment?: false
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Protein
Q62087
Organism: Mus musculus/domesticus
Length: 354  
Fragment?: false
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Protein
P52430
Organism: Mus musculus/domesticus
Length: 355  
Fragment?: false
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Protein
H3BLB8
Organism: Mus musculus/domesticus
Length: 181  
Fragment?: false
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Protein
H3BK03
Organism: Mus musculus/domesticus
Length: 256  
Fragment?: true
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Publication
17379834 | J:135375
First Author: Shih DM
Year: 2007
Journal: Circ Res
Title: Decreased obesity and atherosclerosis in human paraoxonase 3 transgenic mice.
Volume: 100
Issue: 8
Pages: 1200-7
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Publication
12633754 | J:82696
First Author: Rozenberg O
Year: 2003
Journal: Free Radic Biol Med
Title: Paraoxonase (PON1) deficiency is associated with increased macrophage oxidative stress: studies in PON1-knockout mice.
Volume: 34
Issue: 6
Pages: 774-84
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Publication
10421368 | -
First Author: Saito Y
Year: 1999
Journal: Nature
Title: Molecular characterization of the melanin-concentrating-hormone receptor.
Volume: 400
Issue: 6741
Pages: 265-9
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