protein-glucosylgalactosylhydroxylysine glucosidase | |||||||||
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Identifiers | |||||||||
EC no. | 3.2.1.107 | ||||||||
CAS no. | 72829-45-9 | ||||||||
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 protein-glucosylgalactosylhydroxylysine glucosidase (EC 3.2.1.107) catalyzes the following chemical reaction:
It belongs to the family of hydrolases, specifically those glycosidases that hydrolyse O- and S-glycosyl compounds. The systematic name is protein-α-D-glucosyl-1,2-β-D-galactosyl-L-hydroxylysine glucohydrolase. Other names in common use include 2-O-α-D-glucopyranosyl-5-O-α-D-galactopyranosylhydroxy-L-lysine glucohydrolase, and lysine glucohydrolase.
Hydroxylysine (Hyl) is an amino acid with the molecular formula C6H14N2O3. It was first discovered in 1921 by Donald Van Slyke as the 5-hydroxylysine form. It arises from a post-translational hydroxy modification of lysine. It is most widely known as a component of collagen.
In chemistry, hydroxylation can refer to:
Heparan sulfate (HS) is a linear polysaccharide found in all animal tissues. It occurs as a proteoglycan in which two or three HS chains are attached in close proximity to cell surface or extracellular matrix proteins. In this form, HS binds to a variety of protein ligands, including Wnt, and regulates a wide range of biological activities, including developmental processes, angiogenesis, blood coagulation, abolishing detachment activity by GrB, and tumour metastasis. HS has also been shown to serve as cellular receptor for a number of viruses, including the respiratory syncytial virus. One study suggests that cellular heparan sulfate has a role in SARS-CoV-2 Infection, particularly when the virus attaches with ACE2.
β-Glucosidase is an enzyme that catalyses the following reaction:
α-Glucosidase is a glucosidase located in the brush border of the small intestine that acts upon α(1→4) bonds:
Glucan 1,4-α-glucosidase is an enzyme located on the brush border of the small intestine with systematic name 4-α-D-glucan glucohydrolase. It catalyses the following chemical reaction
The enzyme 6-phospho-β-glucosidase (EC 3.2.1.86) catalyzes the following reaction:
In enzymology, a beta-apiosyl-beta-glucosidase (EC 3.2.1.161) is an enzyme that catalyzes the chemical reaction
In enzymology, a glucosylceramidase (EC 3.2.1.45) is an enzyme that catalyzes the chemical reaction
In enzymology, a procollagen galactosyltransferase is an enzyme that catalyzes the chemical reaction
In enzymology, a procollagen glucosyltransferase is an enzyme that catalyzes the chemical reaction
In enzymology, a hydroxylysine kinase is an enzyme that catalyzes the chemical reaction
Momordin is one of several saponins derived from oleanolic acid, a triterpenoid. These chemical compounds are found in some plants of the genus Momordica, which includes the bitter melon and the balsam apple, as well as in other Asian herbal medicine plants such as Kochia scoparia and Ampelopsis radix.
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.
Sucrose α-glucosidase is an enzyme with systematic name sucrose-α-D-glucohydrolase. It catalyses the hydrolysis of sucrose and maltose by an α-D-glucosidase-type action.
Glucan 1,6-α-glucosidase is an enzyme with systematic name glucan 6-α-D-glucohydrolase. It catalyses the hydrolysis of (1→6)-α-D-glucosidic linkages in (1→6)-α-D-glucans and derived oligosaccharides
Mannosyl-oligosaccharide glucosidase (MOGS) (EC 3.2.1.106, processing α-glucosidase I,Glc3Man9NAc2 oligosaccharide glucosidase, trimming glucosidase I, GCS1) is an enzyme with systematic name mannosyl-oligosaccharide glucohydrolase. MOGS is a transmembrane protein found in the membrane of the endoplasmic reticulum of eukaryotic cells. Biologically, it functions within the N-glycosylation pathway.
Branched-dextran exo-1,2-α-glucosidase is an enzyme with systematic name (1→2)-α-D-glucosyl-branched-dextran 2-glucohydrolase. It catalyses the hydrolysis of (1→2)-α-D-glucosidic linkages at the branch points of dextrans and related polysaccharides, producing free D-glucose.
Hesperidin 6-O-alpha-L-rhamnosyl-beta-D-glucosidase (EC 3.2.1.168) is an enzyme with systematic name hesperetin 7-(6-O-alpha-L-rhamnopyranosyl-beta-D-glucopyranoside) 6-O-alpha-rhamnopyranosyl-beta-glucohydrolase. This enzyme catalyses the following chemical reaction
N2-citryl-N6-acetyl-N6-hydroxylysine synthase (EC 6.3.2.38, N(alpha)-citryl-N(epsilon)-acetyl-N(epsilon)-hydroxylysine synthase, iucA (gene)) is an enzyme with systematic name citrate:N6-acetyl-N6-hydroxy-L-lysine ligase (ADP-forming). This enzyme catalyses the following chemical reaction