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Search results 301 to 318 out of 318 for Pon3

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0.017s

Type

Details

Score

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

•

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.

•

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

•

Protein

Q99JS7

Organism:	Mus musculus/domesticus
Length:	108
Fragment?:	false

•

Protein

H3BL07

Organism:	Mus musculus/domesticus
Length:	135
Fragment?:	true

•

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

•

Protein

Q62087

Organism:	Mus musculus/domesticus
Length:	354
Fragment?:	false

•

Protein

P52430

Organism:	Mus musculus/domesticus
Length:	355
Fragment?:	false

•

Protein

H3BLB8

Organism:	Mus musculus/domesticus
Length:	181
Fragment?:	false

•

Protein

H3BK03

Organism:	Mus musculus/domesticus
Length:	256
Fragment?:	true

•

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

•

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

•

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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