Arylesterase: Difference between revisions
Content deleted Content added
m →References: Sort into more specific stub template based on presence in Category:EC 3.1 or subcategories (Task 25) |
|||
| (8 intermediate revisions by 6 users not shown) | |||
| Line 1: | Line 1: | ||
{{enzyme |
{{infobox enzyme |
||
| Name = arylesterase |
| Name = arylesterase |
||
| EC_number = 3.1.1.2 |
| EC_number = 3.1.1.2 |
||
| CAS_number = 9032-73-9 |
| CAS_number = 9032-73-9 |
||
| GO_code = 0004064 |
|||
| IUBMB_EC_number = 3/1/1/2 |
|||
| |
| image = |
||
| |
| width = |
||
| |
| caption = |
||
| caption = |
|||
}} |
}} |
||
The enzyme '''arylesterase''' (EC 3.1.1.2) [[catalysis|catalyzes]] the reaction |
|||
:a phenyl acetate + H<sub>2</sub>O <math>\rightleftharpoons</math> a phenol + acetate |
:a phenyl acetate + H<sub>2</sub>O <math>\rightleftharpoons</math> a phenol + acetate |
||
Thus, the two [[substrate (biochemistry)|substrates]] of this enzyme are [[phenyl acetate]] and [[water|H<sub>2</sub>O]], whereas its two [[product (chemistry)|products]] are [[phenol]] and [[acetate]]. |
|||
This enzyme belongs to the family of [[hydrolase]]s, specifically those acting on carboxylic [[ester]] bonds. The [[List of enzymes|systematic name]] of this enzyme class is '''aryl-ester hydrolase'''. Other names in common use include '''A-esterase''', '''paraoxonase''', and '''aromatic esterase'''. This enzyme participates in [[bisphenol a degradation]]. |
This enzyme belongs to the family of [[hydrolase]]s, specifically those acting on carboxylic [[ester]] bonds. The [[List of enzymes|systematic name]] of this enzyme class is '''aryl-ester hydrolase'''. Other names in common use include '''A-esterase''', '''paraoxonase''', and '''aromatic esterase'''. This enzyme participates in [[bisphenol a degradation]]. |
||
| Line 23: | Line 20: | ||
==References== |
==References== |
||
{{reflist|1}} |
{{reflist|1}} |
||
* {{cite journal | author = ALDRIDGE WN | date = 1953 | title = Serum esterases. |
* {{cite journal | author = ALDRIDGE WN | date = 1953 | title = Serum esterases. I. Two types of esterase (A and B) hydrolysing ''p''-nitrophenyl acetate, propionate and butyrate, and a method for their determination | journal = Biochem. J. | volume = 53 | pages = 110–7 | pmid = 13032041 | issue = 1 | pmc = 1198110 | doi=10.1042/bj0530110}} |
||
* {{cite journal | vauthors = AUGUSTINSSON KB, OLSSON B | date = 1959 | title = Esterases in the milk and blood plasma of swine. I. Substrate specificity and electrophoresis studies | journal = Biochem. J. | volume = 71 | pages = 477–84 | pmid = 13638253 | issue = 3 | pmc = 1196820 }} |
* {{cite journal | vauthors = AUGUSTINSSON KB, OLSSON B | date = 1959 | title = Esterases in the milk and blood plasma of swine. I. Substrate specificity and electrophoresis studies | journal = Biochem. J. | volume = 71 | pages = 477–84 | pmid = 13638253 | issue = 3 | doi = 10.1042/bj0710477 | pmc = 1196820 }} |
||
* {{cite journal | author = Bosmann HB | date = 1972 | title = Membrane marker enzymes. Characterization of an arylesterase of guinea pig cerebral cortex utilizing p-nitrophenyl acetate as substrate | journal = Biochim. Biophys. Acta | volume = 276 | pages = 180–91 | pmid = 5047702 | issue = 1 | doi=10.1016/0005-2744(72)90019-8}} |
* {{cite journal | author = Bosmann HB | date = 1972 | title = Membrane marker enzymes. Characterization of an arylesterase of guinea pig cerebral cortex utilizing ''p''-nitrophenyl acetate as substrate | journal = Biochim. Biophys. Acta | volume = 276 | pages = 180–91 | pmid = 5047702 | issue = 1 | doi=10.1016/0005-2744(72)90019-8}} |
||
* {{cite journal | vauthors = Kim DH, Yang YS, Jakoby WB | date = 1990 | title = Nonserine esterases from rat liver cytosol | journal = Protein |
* {{cite journal | vauthors = Kim DH, Yang YS, Jakoby WB | date = 1990 | title = Nonserine esterases from rat liver cytosol | journal = Protein Expr. Purif. | volume = 1 | pages = 19–27 | pmid = 2152179 | doi = 10.1016/1046-5928(90)90040-6 | issue = 1 }} |
||
* {{cite journal | vauthors = Mackness MI, Thompson HM, Hardy AR, Walker CH | date = 1987 | title = Distinction between 'A'-esterases and arylesterases. Implications for esterase classification | journal = Biochem. J. | volume = 245 | pages = 293–6 | pmid = 2822017 | issue = 1 | pmc = 1148115 }} |
* {{cite journal | vauthors = Mackness MI, Thompson HM, Hardy AR, Walker CH | date = 1987 | title = Distinction between 'A'-esterases and arylesterases. Implications for esterase classification | journal = Biochem. J. | volume = 245 | pages = 293–6 | pmid = 2822017 | issue = 1 | pmc = 1148115 | doi=10.1042/bj2450293}} |
||
* {{cite journal | vauthors = Khersonsky O, Tawfik DS | date = Apr 2005| title = Structure-reactivity studies of serum paraoxonase PON1 suggest that its native activity is lactonase.| |
* {{cite journal | vauthors = Khersonsky O, Tawfik DS | date = Apr 2005| title = Structure-reactivity studies of serum paraoxonase PON1 suggest that its native activity is lactonase.|pmid=15835926 | journal = Biochemistry | volume = 44| issue = 16| pages = 6371–82| doi=10.1021/bi047440d}} |
||
* {{cite journal | date = June 2005| title = Human paraoxonases (PON1, PON2, and PON3) are lactonases with overlapping and distinct substrate specificities| |
* {{cite journal | date = June 2005| title = Human paraoxonases (PON1, PON2, and PON3) are lactonases with overlapping and distinct substrate specificities|pmid=15772423 | vauthors = Draganov DI, Teiber JF, Speelman A, Osawa Y, Sunahara R, La Du BN | volume = 46| pages = 1239–47| doi=10.1194/jlr.M400511-JLR200 | journal=J. Lipid Res.| issue = 6| doi-access =free}} |
||
* {{cite journal | doi = 10.1194/jlr.m400511-jlr200 | volume=46 | title=Human paraoxonases (PON1, PON2, and PON3) are lactonases with overlapping and distinct substrate specificities | journal=The Journal of Lipid Research | pages=1239–1247}} |
* {{cite journal | doi = 10.1194/jlr.m400511-jlr200 | volume=46 | title=Human paraoxonases (PON1, PON2, and PON3) are lactonases with overlapping and distinct substrate specificities | journal=The Journal of Lipid Research | pages=1239–1247 | pmid=15772423 | date=June 2005 | vauthors=Draganov DI, Teiber JF, Speelman A, Osawa Y, Sunahara R, La Du BN| issue=6 | doi-access=free }} |
||
{{Esterases}} |
{{Esterases}} |
||
{{Enzymes}} |
{{Enzymes}} |
||
{{Portal bar| |
{{Portal bar|Biology|border=no}} |
||
[[Category:EC 3.1.1]] |
[[Category:EC 3.1.1]] |
||
Latest revision as of 13:14, 26 August 2023
| arylesterase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.1.1.2 | ||||||||
| CAS no. | 9032-73-9 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
The enzyme arylesterase (EC 3.1.1.2) catalyzes the reaction
- a phenyl acetate + H2O a phenol + acetate
This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name of this enzyme class is aryl-ester hydrolase. Other names in common use include A-esterase, paraoxonase, and aromatic esterase. This enzyme participates in bisphenol a degradation.
Structural studies
[edit]As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 1V04 and 1VA4.
References
[edit]- ALDRIDGE WN (1953). "Serum esterases. I. Two types of esterase (A and B) hydrolysing p-nitrophenyl acetate, propionate and butyrate, and a method for their determination". Biochem. J. 53 (1): 110–7. doi:10.1042/bj0530110. PMC 1198110. PMID 13032041.
- AUGUSTINSSON KB, OLSSON B (1959). "Esterases in the milk and blood plasma of swine. I. Substrate specificity and electrophoresis studies". Biochem. J. 71 (3): 477–84. doi:10.1042/bj0710477. PMC 1196820. PMID 13638253.
- Bosmann HB (1972). "Membrane marker enzymes. Characterization of an arylesterase of guinea pig cerebral cortex utilizing p-nitrophenyl acetate as substrate". Biochim. Biophys. Acta. 276 (1): 180–91. doi:10.1016/0005-2744(72)90019-8. PMID 5047702.
- Kim DH, Yang YS, Jakoby WB (1990). "Nonserine esterases from rat liver cytosol". Protein Expr. Purif. 1 (1): 19–27. doi:10.1016/1046-5928(90)90040-6. PMID 2152179.
- Mackness MI, Thompson HM, Hardy AR, Walker CH (1987). "Distinction between 'A'-esterases and arylesterases. Implications for esterase classification". Biochem. J. 245 (1): 293–6. doi:10.1042/bj2450293. PMC 1148115. PMID 2822017.
- Khersonsky O, Tawfik DS (Apr 2005). "Structure-reactivity studies of serum paraoxonase PON1 suggest that its native activity is lactonase". Biochemistry. 44 (16): 6371–82. doi:10.1021/bi047440d. PMID 15835926.
- Draganov DI, Teiber JF, Speelman A, Osawa Y, Sunahara R, La Du BN (June 2005). "Human paraoxonases (PON1, PON2, and PON3) are lactonases with overlapping and distinct substrate specificities". J. Lipid Res. 46 (6): 1239–47. doi:10.1194/jlr.M400511-JLR200. PMID 15772423.
- Draganov DI, Teiber JF, Speelman A, Osawa Y, Sunahara R, La Du BN (June 2005). "Human paraoxonases (PON1, PON2, and PON3) are lactonases with overlapping and distinct substrate specificities". The Journal of Lipid Research. 46 (6): 1239–1247. doi:10.1194/jlr.m400511-jlr200. PMID 15772423.
