Glucarolactone O-hydroxycinnamoyltransferase

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glucarolactone O-hydroxycinnamoyltransferase
Identifiers
EC no. 2.3.1.132
CAS no. 112956-52-2
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In enzymology, a glucarolactone O-hydroxycinnamoyltransferase (EC 2.3.1.132) is an enzyme that catalyzes the chemical reaction

sinapoyl-CoA + glucarolactone CoA + O-sinapoylglucarolactone

Thus, the two substrates of this enzyme are sinapoyl-CoA and glucarolactone, whereas its two products are CoA and O-sinapoylglucarolactone.

This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is sinapoyl-CoA:glucarolactone O-(hydroxycinnamoyl)transferase.

Related Research Articles

<span class="mw-page-title-main">Transferase</span> Class of enzymes

A transferase is any one of a class of enzymes that catalyse the transfer of specific functional groups from one molecule to another. They are involved in hundreds of different biochemical pathways throughout biology, and are integral to some of life's most important processes.

The peptidyl transferase is an aminoacyltransferase as well as the primary enzymatic function of the ribosome, which forms peptide bonds between adjacent amino acids using tRNAs during the translation process of protein biosynthesis. The substrates for the peptidyl transferase reaction are two tRNA molecules, one bearing the growing peptide chain and the other bearing the amino acid that will be added to the chain. The peptidyl chain and the amino acids are attached to their respective tRNAs via ester bonds to the O atom at the CCA-3' ends of these tRNAs. Peptidyl transferase is an enzyme that catalyzes the addition of an amino acid residue in order to grow the polypeptide chain in protein synthesis. It is located in the large ribosomal subunit, where it catalyzes the peptide bond formation. It is composed entirely of RNA. The alignment between the CCA ends of the ribosome-bound peptidyl tRNA and aminoacyl tRNA in the peptidyl transferase center contribute to its ability to catalyze these reactions. This reaction occurs via nucleophilic displacement. The amino group of the aminoacyl tRNA attacks the terminal carboxyl group of the peptidyl tRNA. Peptidyl transferase activity is carried out by the ribosome. Peptidyl transferase activity is not mediated by any ribosomal proteins but by ribosomal RNA (rRNA), a ribozyme. Ribozymes are the only enzymes which are not made up of proteins, but ribonucleotides. All other enzymes are made up of proteins. This RNA relic is the most significant piece of evidence supporting the RNA World hypothesis.

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<span class="mw-page-title-main">Homocitrate synthase</span> Enzyme

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In enzymology, a sinapoylglucose---choline O-sinapoyltransferase is an enzyme that catalyzes the chemical reaction

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References


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