1-aminocyclopropane-1-carboxylate deaminase

1-aminocyclopropane-1-carboxylate deaminase

In enzymology, a 1-aminocyclopropane-1-carboxylate deaminase (EC number|3.5.99.7) is an enzyme that catalyzes the chemical reaction

:1-aminocyclopropane-1-carboxylate + H2O ightleftharpoons 2-oxobutanoate + NH3

Thus, the two substrates of this enzyme are 1-aminocyclopropane-1-carboxylate and H2O, whereas its two products are 2-oxobutanoate and NH3.

This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in compounds that have not been otherwise categorized within EC number 3.5. The systematic name of this enzyme class is 1-aminocyclopropane-1-carboxylate aminohydrolase (isomerizing). This enzyme is also called 1-aminocyclopropane-1-carboxylate endolyase (deaminating). This enzyme participates in propanoate metabolism. It employs one cofactor, pyridoxal phosphate.

tructural studies

As of late 2007, 6 structures have been solved for this class of enzymes, with PDB accession codes PDB link|1RQX, PDB link|1TYZ, PDB link|1TZ2, PDB link|1TZJ, PDB link|1TZK, and PDB link|1TZM.

References

*
*

External links

::"The CAS registry number for this enzyme class is CAS registry|69553-48-6."

Gene Ontology (GO) codes


Wikimedia Foundation. 2010.

Игры ⚽ Поможем сделать НИР

Look at other dictionaries:

  • List of EC numbers (EC 3) — This list contains a list of EC numbers for the third group, EC 3, hydrolases, placed in numerical order as determined by the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology.EC 3.1: Acting on Ester BondsEC… …   Wikipedia

  • Pseudomonas brassicacearum — Taxobox color = lightgrey name = Pseudomonas brassicacearum image width = 240px image caption = regnum = Bacteria phylum = Proteobacteria classis = Gamma Proteobacteria ordo = Pseudomonadales familia = Pseudomonadaceae genus = Pseudomonas species …   Wikipedia

Share the article and excerpts

Direct link
Do a right-click on the link above
and select “Copy Link”