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Hydrolases can be further classified into several subclasses, based upon the bonds they act upon: EC 3.1: ester bonds (esterases: nucleases, phosphodiesterases, lipase, phosphatase) EC 3.2: sugars (DNA glycosylases, glycoside hydrolase) EC 3.3: ether bonds; EC 3.4: peptide bonds (Proteases/peptidases) EC 3.5: carbon-nitrogen bonds, other than ...
An ester of carboxylic acid. R stands for any group (organic or inorganic) and R′ stands for organyl group. In chemistry, an ester is a compound derived from an acid (organic or inorganic) in which the hydrogen atom (H) of at least one acidic hydroxyl group (−OH) of that acid is replaced by an organyl group (−R).
The enzyme protein-glutamate methylesterase (EC 3.1.1.61) catalyzes the reaction . protein L-glutamate O 5-methyl ester + H 2 O protein L-glutamate + methanol. This enzyme is a demethylase, and more specifically it belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds.
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 ...
EC 3.1.2: Thiolester hydrolases. Thioesterase. Ubiquitin carboxy-terminal hydrolase L1; EC 3.1.3: Phosphoric monoester hydrolases. Phosphatase (EC 3.1.3.x), hydrolyses phosphoric acid monoesters into a phosphate ion and an alcohol Alkaline phosphatase, removes phosphate groups from many types of molecules, including nucleotides, proteins, and ...
The "bond" involves this linkage C−O−PO − 2 O−C. [1] Discussion of phosphodiesters is dominated by their prevalence in DNA and RNA, but phosphodiesters occur in other biomolecules, e.g. acyl carrier proteins, phospholipids and the cyclic forms of GMP and AMP (cGMP and cAMP). [2]
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:
The result of this sequential cascade is to bind ubiquitin to lysine residues on the protein substrate via an isopeptide bond, cysteine residues through a thioester bond; serine, threonine, and tyrosine residues through an ester bond; or the amino group of the protein's N-terminus via a peptide bond. [7] [8] [9] [10]