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The structure and function of paraoxonase-1 and its comparison to paraoxonase-2 and -3
ID
Taler-Verčič, Ajda
(
Avtor
),
ID
Goličnik, Marko
(
Avtor
),
ID
Bavec, Aljoša
(
Avtor
)
PDF - Predstavitvena datoteka,
prenos
(10,81 MB)
MD5: 32A76A196C0635BF3051D478095891A5
URL - Izvorni URL, za dostop obiščite
https://www.mdpi.com/1420-3049/25/24/5980
Galerija slik
Izvleček
Serum paraoxonase-1 (PON1) is the most studied member of the group of paraoxonases (PONs). This enzyme possesses three enzymatic activities: lactonase, arylesterase, and paraoxonase activity. PON1 and its isoforms play an important role in drug metabolism as well as in the prevention of cardiovascular and neurodegenerative diseases. Although all three members of the PON family have the same origin and very similar amino acid sequences, they have different functions and are found in different locations. PONs exhibit substrate promiscuity, and their true physiological substrates are still not known. However, possible substrates include homocysteine thiolactone, an analogue of natural quorum-sensing molecules, and the recently discovered derivatives of arachidonic acid—bioactive δ-lactones. Directed evolution, site-directed mutagenesis, and kinetic studies provide comprehensive insights into the active site and catalytic mechanism of PON1. However, there is still a whole world of mystery waiting to be discovered, which would elucidate the substrate promiscuity of a group of enzymes that are so similar in their evolution and sequence yet so distinct in their function.
Jezik:
Angleški jezik
Ključne besede:
paraoxonase
,
lactonase
,
oxidative stress
,
PON1
,
PON2
,
PON3
,
arylesterase
,
organophosphate
,
structure
,
kinetic
,
atherosclerosis
Vrsta gradiva:
Članek v reviji
Tipologija:
1.02 - Pregledni znanstveni članek
Organizacija:
MF - Medicinska fakulteta
Status publikacije:
Objavljeno
Različica publikacije:
Objavljena publikacija
Leto izida:
2020
Št. strani:
20 str.
Številčenje:
Vol. 25, iss. 24, art. 5980
PID:
20.500.12556/RUL-134835
UDK:
577
ISSN pri članku:
1420-3049
DOI:
10.3390/molecules25245980
COBISS.SI-ID:
43242755
Datum objave v RUL:
03.02.2022
Število ogledov:
849
Število prenosov:
147
Metapodatki:
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Objavi na:
Gradivo je del revije
Naslov:
Molecules
Skrajšan naslov:
Molecules
Založnik:
MDPI
ISSN:
1420-3049
COBISS.SI-ID:
18462981
Licence
Licenca:
CC BY 4.0, Creative Commons Priznanje avtorstva 4.0 Mednarodna
Povezava:
http://creativecommons.org/licenses/by/4.0/deed.sl
Opis:
To je standardna licenca Creative Commons, ki daje uporabnikom največ možnosti za nadaljnjo uporabo dela, pri čemer morajo navesti avtorja.
Začetek licenciranja:
17.12.2020
Sekundarni jezik
Jezik:
Slovenski jezik
Ključne besede:
paraoksonaza
,
laktonaza
,
oksidativni stres
Projekti
Financer:
ARRS - Agencija za raziskovalno dejavnost Republike Slovenije
Številka projekta:
P1-0170
Naslov:
Molekulski mehanizmi uravnavanja celičnih procesov v povezavi z nekaterimi boleznimi pri človeku
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