AB Hydrolase
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AB Hydrolase
The alpha/beta hydrolase superfamily is a Protein superfamily, superfamily of hydrolytic enzymes of widely differing phylogenetic origin and catalytic function that share a common Protein fold, fold. The core of each enzyme is an alpha/beta-sheet (rather than a beta barrel, barrel), containing 8 beta strands connected by 6 alpha helix, alpha helices. The enzymes are believed to have diverged from a common ancestor, retaining little obvious sequence similarity, but preserving the arrangement of the catalytic residues. All have a catalytic triad, the elements of which are borne on loops, which are the best-conserved structural features of the fold. The alpha/beta hydrolase fold includes proteases, lipases, peroxidases, esterases, epoxide hydrolases and dehalogenases. Database The ESTHER database provides a large collection of information about this superfamily of proteins. Subfamilies *3-oxoadipate enol-lactonase Human proteins containing this domain ABHD10; ABHD11; ABHD12; A ...
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Lipase
Lipase ( ) is a family of enzymes that catalyzes the hydrolysis of fats. Some lipases display broad substrate scope including esters of cholesterol, phospholipids, and of lipid-soluble vitamins and sphingomyelinases; however, these are usually treated separately from "conventional" lipases. Unlike esterases, which function in water, lipases "are activated only when adsorbed to an oil–water interface". Lipases perform essential roles in digestion, transport and processing of dietary lipids in most, if not all, organisms. Structure and catalytic mechanism Classically, lipases catalyse the hydrolysis of triglycerides: :triglyceride + H2O → fatty acid + diacylglycerol :diacylglycerol + H2O → fatty acid + monacylglycerol :monacylglycerol + H2O → fatty acid + glycerol Lipases are serine hydrolases, i.e. they function by transesterification generating an acyl serine intermediate. Most lipases act at a specific position on the glycerol backbone of a lipid sub ...
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ABHD11
Abhydrolase domain-containing protein 11 also known as Williams-Beuren syndrome chromosomal region 21 protein (WBSCR21) is an enzyme that in humans is encoded by the ''ABHD11'' gene. This gene encodes a protein containing an alpha/beta hydrolase fold domain. This gene is deleted in Williams syndrome, a multisystem developmental disorder caused by the deletion of contiguous genes at 7q11.23. Alternatively spliced transcript variants have been described, but their biological validity has not been determined. References External links * Further reading * * * * * EC 3.1 {{gene-7-stub ...
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BAT5
Protein BAT5 is a protein that in humans is encoded by the ''BAT5'' gene. A cluster of genes, BAT1-BAT5, has been localized in the vicinity of the genes for TNF alpha and TNF beta. These genes are all within the human major histocompatibility complex class III region. The protein encoded by this gene is thought to be involved in some aspects of immunity. Bat5 structure Amino acid sequence The human BAT5 protein (also known as ABHD16A) is 558 amino acid residues long. It was first identified in 1992 in the gene domains of TNF alpha and TNF beta. The BAT5 (ABHD 16A) proteins found in different species have varying lengths. BAT5 is highly conserved in human, mice and other mammals. It is found to be expressed in multiple different tissue cells. According to molecular evolutionary genetic analysis, in comparison of 13 mammalian species, it was denoted that the differences in amino acid sequence length are due to splicing in the post transcriptional processing of mRNA. ...
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ABHD6
alpha/beta-Hydrolase domain containing 6 (ABHD6), also known as monoacylglycerol lipase ABHD6 or 2-arachidonoylglycerol hydrolase is an enzyme that in humans is encoded by the ABHD6 gene. Function ABHD6 is a serine hydrolyzing enzyme that possesses typical α/β-hydrolase family domains. ABHD6 was first studied because of its over-expression in certain forms of tumours. ABHD6 has been linked to regulation of the endocannabinoid system as it controls the accumulation of 2-arachidonoylglycerol (2-AG) at the cannabinoid receptors. ABHD6 accounts for about 4% of 2-AG brain hydrolysis. Together, monoacylglycerol lipase (MAGL), ABHD12, and ABHD6 control about 99% of 2-AG signalling in the brain, and each enzyme exhibits a distinct subcellular distribution, suggesting that they regulate distinct pools of 2-AG in the nervous system. See also * Fatty acid amide hydrolase Fatty acid amide hydrolase or FAAH (, oleamide hydrolase, anandamide amidohydrolase) is a member of the serin ...
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ABHD5
1-acylglycerol-3-phosphate O-acyltransferase ABHD5 is an enzyme that in humans is encoded by the ''ABHD5'' gene. Function The protein encoded by this gene belongs to a large family of proteins defined by an alpha/beta hydrolase fold, and contains three sequence motifs that correspond to a catalytic triad found in the esterase/lipase/thioesterase subfamily. It differs from other members of this subfamily in that its putative catalytic triad contains an asparagine instead of the serine residue. Mutations in this gene have been associated with Chanarin-Dorfman syndrome, a triglyceride storage disease with impaired long-chain fatty acid oxidation. Model organisms Model organisms have been used in the study of ABHD5 function. A conditional knockout mouse line, called ''Abhd5tm1a(KOMP)Wtsi'' was generated as part of the International Knockout Mouse Consortium program — a high-throughput mutagenesis project to generate and distribute animal models of disease to interested scientist ...
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ABHD3
Alpha/beta hydrolase domain containing 3 (ABHD3; alternative names: lung alpha/beta hydrolase 3, phospholipase ABHD3) is a single pass type II membrane member of the serine hydrolase family of enzymes. The expression of murine ABHD3 is highest in the brain, liver, and kidney. ABHD3 hydrolytic activity is highly specific for medium chain (e.g., dimyristoylphosphatidylcholine) and oxidatively truncated (e.g., azelaoyl PAF) phospholipids. ABHD3-deficient mice are viable, fertile, and possess dramatically elevated medium chain phospholipids in tissues and in blood. Conversely, ectopic expression of ABHD3 prevents the accumulation of oxidized phospholipids Phospholipids, are a class of lipids whose molecule has a hydrophilic "head" containing a phosphate group and two hydrophobic "tails" derived from fatty acids, joined by an alcohol residue (usually a glycerol molecule). Marine phospholipids typ ... in cells. References {{Reflist Enzymes Hydrolases ...
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ABHD2
Abhydrolase domain-containing protein 2 is a serine hydrolase enzyme that is strongly expressed in human spermatozoa. It is a key controller of sperm hyperactivation, which is a necessary step in allowing sperm to fertilize an egg. It is encoded by the ''ABHD2'' gene. Function In the presence of Progesterone (or Pregnenolone Sulfate,) it cleaves 2-arachidonoylglycerol (2AG) into glycerol and arachidonic acid (AA). 2AG inhibits sperm calcium channel CatSper, and so when ABHD2 removes 2AG calcium flows into the cell through the CatSper channel, leading to hyperactivation. ABHD2 is inhibited by testosterone, (as well as hydrocortisone, and the plant triterpenoids lupeol and pristimerin) which may prevent premature hyperactivation. Structure This gene encodes a protein containing an alpha/beta hydrolase fold, which is a catalytic domain found in a very wide range of enzymes. Alternative splicing of this gene results in two transcript variants encoding the same protein. Role ...
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