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Cutinase has an assigned enzyme commission number of EC 3.1.1.74. [2] Cutinase is in the third class of enzymes, meaning that its primary function is to hydrolyze its substrate (in this case, cutin). [3] Within the third class, cutinase is further categorized into the first subclass, which indicates that it specifically hydrolyzes ester bonds. [2]
Once in position, the water molecule acts as a nucleophile, and attacks the carbonyl group of the ester bond between the nascent protein and the tRNA. The hydrolysis of the ester bond causes the release of the nascent protein and the disassembly of the ribosome and termination complex. [37] Hydrolysis of ester bond to release nascent protein [37]
Ether phospholipids: phospholipids are known to have ether-linked "tails" instead of the usual ester linkage. [1] Ether on sn-1, ester on sn-2: "ether lipids" in the context of bacteria and eukaryotes refer to this class of lipids. Compared to the usual 1,2-diacyl-sn-glycerol (DAG), the sn-1 linkage is replaced with an ester bond. [1] [2] [3]
Chlorophyllase can be found in the chloroplast, thylakoid membrane and etioplast of at least higher plants such as ferns, mosses, brown and red algae and diatoms. Chlase is the catalyst for the hydrolysis of chlorophyll to produce chlorophyllide (also called Chlide) and phytol .
1071 n/a Ensembl ENSG00000087237 n/a UniProt P11597 n/a RefSeq (mRNA) NM_000078 NM_001286085 n/a RefSeq (protein) NP_000069 NP_001273014 n/a Location (UCSC) Chr 16: 56.96 – 56.98 Mb n/a PubMed search n/a Wikidata View/Edit Human Cholesteryl ester transfer protein (CETP), also called plasma lipid transfer protein, is a plasma protein that facilitates the transport of cholesteryl esters and ...
However, additional molecular interactions may render the amide form less stable; the amino group is expelled instead, resulting in an ester (Ser/Thr) or thioester (Cys) bond in place of the peptide bond. This chemical reaction is called an N-O acyl shift. The ester/thioester bond can be resolved in several ways:
This linkage is an ester bond that chemically binds the carboxyl group of an amino acid to the terminal 3'-OH group of its cognate tRNA. [7] It has been discovered that the amino acid moiety of a given aa-tRNA provides for its structural integrity; the tRNA moiety dictates, for the most part, how and when the amino acid will be incorporated ...
Cross-sectional view of the structures that can be formed by phospholipids in an aqueous solution. A biological membrane, biomembrane or cell membrane is a selectively permeable membrane that separates the interior of a cell from the external environment or creates intracellular compartments by serving as a boundary between one part of the cell and another.