1,4-lactonase | |||||||||
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Identifiers | |||||||||
EC no. | 3.1.1.25 | ||||||||
CAS no. | 37278-38-9 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
Gene Ontology | AmiGO / QuickGO | ||||||||
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The enzyme 1,4-lactonase (EC 3.1.1.25) catalyzes the generic reaction
This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name is 1,4-lactone hydroxyacylhydrolase. It is also called γ-lactonase. It participates in galactose metabolism and ascorbate and aldarate metabolism. It employs one cofactor, Ca2+.
As of late 2007, three structures have been solved for this class of enzymes, with PDB accession codes 2DG0, 2DG1, and 2DSO.
In a study by Chen et al. a 1,4-lactonase was expressed in E. coli and used as a highly efficient biocatalyst for asymmetric synthesis of chiral compounds. [1]
A debranching enzyme is a molecule that helps facilitate the breakdown of glycogen, which serves as a store of glucose in the body, through glucosyltransferase and glucosidase activity. Together with phosphorylases, debranching enzymes mobilize glucose reserves from glycogen deposits in the muscles and liver. This constitutes a major source of energy reserves in most organisms. Glycogen breakdown is highly regulated in the body, especially in the liver, by various hormones including insulin and glucagon, to maintain a homeostatic balance of blood-glucose levels. When glycogen breakdown is compromised by mutations in the glycogen debranching enzyme, metabolic diseases such as Glycogen storage disease type III can result.
Monoacylglycerol lipase is an enzyme that, in humans, is encoded by the MGLL gene. MAGL is a 33-kDa, membrane-associated member of the serine hydrolase superfamily and contains the classical GXSXG consensus sequence common to most serine hydrolases. The catalytic triad has been identified as Ser122, His269, and Asp239.
In enzymology, an unspecific monooxygenase (EC 1.14.14.1) is an enzyme that catalyzes the chemical reaction
In enzymology, an (S)-2-hydroxy-acid oxidase (EC 1.1.3.15) is an enzyme that catalyzes the chemical reaction
In enzymology, a lactaldehyde dehydrogenase (EC 1.2.1.22) is an enzyme that catalyzes the chemical reaction
The enzyme 4-hydroxy-2-oxoglutarate aldolase catalyzes the chemical reaction
In enzymology, an arginine—tRNA ligase is an enzyme that catalyzes the chemical reaction
The enzyme (S)-2-methylmalate dehydratase (EC 4.2.1.34) catalyzes the chemical reaction:
The enzyme carboxylesterase (or carboxylic-ester hydrolase, EC 3.1.1.1; systematic name carboxylic-ester hydrolase) catalyzes reactions of the following form:
The enzyme dGTPase (EC 3.1.5.1) catalyzes the reaction
The enzyme gluconolactonase (EC 3.1.1.17) catalyzes the reaction
The enzyme inositol-1,4-bisphosphate 1-phosphatase (EC 3.1.3.57) catalyzes the reaction
The enzyme L-rhamnono-1,4-lactonase (EC 3.1.1.65) catalyzes the reaction
The enzyme lysophospholipase (EC 3.1.1.5) catalyzes the reaction
In enzymology, a galactosyldiacylglycerol alpha-2,3-sialyltransferase is an enzyme that catalyzes the chemical reaction
In enzymology, a glycerate kinase is an enzyme that catalyzes the chemical reaction
In enzymology, a guanylate kinase is an enzyme that catalyzes the chemical reaction
Lactonase (EC 3.1.1.81, acyl-homoserine lactonase; systematic name N-acyl-L-homoserine-lactone lactonohydrolase) is a metalloenzyme, produced by certain species of bacteria, which targets and inactivates acylated homoserine lactones (AHLs). It catalyzes the reaction
2-acyl-sn-glycero-3-phosphocholines are a class of phospholipids that are intermediates in the metabolism of lipids. Because they result from the hydrolysis of an acyl group from the sn-1 position of phosphatidylcholine, they are also called 1-lysophosphatidylcholine. The synthesis of phosphatidylcholines with specific fatty acids occurs through the synthesis of 1-lysoPC. The formation of various other lipids generates 1-lysoPC as a by-product.
Carnitine biosynthesis is a method for the endogenous production of L-carnitine, a molecule that is essential for energy metabolism. In humans and many other animals, L-carnitine is obtained from both diet and by biosynthesis. The carnitine biosynthesis pathway is highly conserved among many eukaryotes and some prokaryotes.