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词条 2-hydroxymuconate-semialdehyde hydrolase
释义

  1. Structural studies

  2. References

{{enzyme
| Name = 2-hydroxymuconate-semialdehyde hydrolase
| EC_number = 3.7.1.9
| CAS_number = 54004-61-4
| IUBMB_EC_number = 3/7/1/9
| GO_code = 0018775
| image =
| width =
| caption =
}}

In enzymology, a 2-hydroxymuconate-semialdehyde hydrolase ({{EC number|3.7.1.9}}) is an enzyme that catalyzes the chemical reaction

2-hydroxymuconate semialdehyde + H2O formate + 2-oxopent-4-enoate

Thus, the two substrates of this enzyme are 2-hydroxymuconate semialdehyde and H2O, whereas its two products are formate and 2-oxopent-4-enoate.

This enzyme belongs to the family of hydrolases, specifically those acting on carbon-carbon bonds in ketonic substances. The systematic name of this enzyme class is 2-hydroxymuconate-semialdehyde formylhydrolase. Other names in common use include 2-hydroxy-6-oxohepta-2,4-dienoate hydrolase, 2-hydroxymuconic semialdehyde hydrolase, HMSH, and HOD hydrolase. This enzyme participates in 5 metabolic pathways: benzoate degradation via hydroxylation, toluene and xylene degradation, 1,4-dichlorobenzene degradation, carbazole degradation, and styrene degradation.

Structural studies

As of late 2007, 10 structures have been solved for this class of enzymes, with PDB accession codes {{PDB link|1IUN}}, {{PDB link|1IUO}}, {{PDB link|1IUP}}, {{PDB link|1UK6}}, {{PDB link|1UK7}}, {{PDB link|1UK8}}, {{PDB link|1UK9}}, {{PDB link|1UKA}}, {{PDB link|1UKB}}, and {{PDB link|2D0D}}.

References

  • {{cite journal |vauthors=Harayama S, Rekik M, Wasserfallen A, Bairoch A | date = 1987 | title = Evolutionary relationships between catabolic pathways for aromatics: conservtion of gene order and nucleotide sequences of catechol oxidation genes of pWW0 and NAH7 plasmids | journal = MGG Mol. Gen. Genet. | volume = 210 | pages = 241–247 | doi = 10.1007/BF00325689 | issue = 2 }}
  • {{cite journal |vauthors=Sala-Trepat JM, Evans WC | date = 1971 | title = The meta cleavage of catechol by Azotobacter species 4-Oxalocrotonate pathway | journal = Eur. J. Biochem. | volume = 20 | pages = 400–13 | pmid = 4325686 | doi = 10.1111/j.1432-1033.1971.tb01406.x | issue = 3 }}
{{Carbon-carbon hydrolases}}{{Enzymes}}{{Portal bar|Molecular and Cellular Biology|border=no}}{{hydrolase-stub}}

2 : EC 3.7.1|Enzymes of known structure

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