请输入您要查询的百科知识:

 

词条 Phosphonoacetaldehyde hydrolase
释义

  1. Structural studies

  2. References

  3. External links

{{enzyme
| Name = phosphonoacetaldehyde hydrolase
| EC_number = 3.11.1.1
| CAS_number = 37289-42-2
| IUBMB_EC_number = 3/11/1/1
| GO_code = 0050194
| image =
| width =
| caption =
}}

In enzymology, a phosphonoacetaldehyde hydrolase ({{EC number|3.11.1.1}}) is an enzyme that catalyzes the chemical reaction

phosphonoacetaldehyde + H2O acetaldehyde + phosphate

Thus, the two substrates of this enzyme are phosphonoacetaldehyde and H2O, whereas its two products are acetaldehyde and phosphate.

This enzyme belongs to the family of hydrolases, specifically those acting on carbon-phosphorus bonds. The systematic name of this enzyme class is 2-oxoethylphosphonate phosphonohydrolase. Other names in common use include phosphonatase, and 2-phosphonoacetylaldehyde phosphonohydrolase. This enzyme participates in aminophosphonate metabolism.

Structural studies

As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes {{PDB link|1SWV}} and {{PDB link|1SWW}}.

References

  • {{cite journal | vauthors = La Nauze JM, Rosenberg H | date = 1968 | title = The identification of 2-phosphonoacetaldehyde as an intermediate in the degradation of 2-aminoethylphosphonate by Bacillus cereus | journal = Biochim. Biophys. Acta | volume = 165 | pages = 438–47 | pmid = 4982500 | issue = 3 | doi=10.1016/0304-4165(68)90223-7}}
  • {{cite journal | vauthors = La Nauze JM, Rosenberg H, Shaw DC | date = 1970 | title = The enzymic cleavage of the carbon-phosphorus bond: purification and properties of phosphonatase | journal = Biochim. Biophys. Acta | volume = 212 | pages = 332–50 | pmid = 4989158 | issue = 2 | doi=10.1016/0005-2744(70)90214-7}}
  • {{cite journal | vauthors = La Nauze JM, Coggins JR, Dixon HB | date = 1977 | title = Aldolase-like imine formation in the mechanism of action of phosphonoacetaldehyde hydrolase | journal = Biochem. J. | volume = 165 | pages = 409–11 | pmid = 200222 | issue = 2 | pmc = 1164914 | doi = 10.1042/bj1650409 }}
  • {{cite journal | vauthors = Olsen DB, Hepburn TW, Moos M, Mariano PS, Dunaway-Mariano D | date = 1988 | title = Investigation of the Bacillus cereus phosphonoacetaldehyde hydrolase. Evidence for a Schiff base mechanism and sequence analysis of an active-site peptide containing the catalytic lysine residue | journal = Biochemistry | volume = 27 | pages = 2229–34 | pmid = 3132206 | doi = 10.1021/bi00406a063 | issue = 6 }}
  • {{cite journal | vauthors = Martin BM, Dunaway-Mariano D | date = 1998 | title = Insights into the mechanism of catalysis by the P-C bond-cleaving enzyme phosphonoacetaldehyde hydrolase derived from gene sequence analysis and mutagenesis | journal = Biochemistry | volume = 37 | pages = 9305–15 | pmid = 9649311 | doi = 10.1021/bi972677d | issue = 26 }}

External links

  • {{Commonscatinline}}
{{enzymes}}{{Portal bar|Molecular and Cellular Biology|border=no}}{{hydrolase-stub}}

2 : EC 3.11.1|Enzymes of known structure

随便看

 

开放百科全书收录14589846条英语、德语、日语等多语种百科知识,基本涵盖了大多数领域的百科知识,是一部内容自由、开放的电子版国际百科全书。

 

Copyright © 2023 OENC.NET All Rights Reserved
京ICP备2021023879号 更新时间:2024/9/21 14:42:04