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Glycosyltransferases are enzymes that establish natural glycosidic linkages. They catalyze the transfer of saccharide moieties from an activated nucleotide sugar to a nucleophilic glycosyl acceptor molecule, the nucleophile of which can be oxygen- carbon-, nitrogen-, or sulfur-based.
Phosphoglycerate kinase is an enzyme that catalyzes the reversible transfer of a phosphate group from 1,3-bisphosphoglycerate (1,3-BPG) to ADP producing 3-phosphoglycerate (3-PG) and ATP :
Phosphoglycerate mutase (PGM) is any enzyme that catalyzes step 8 of glycolysis - the internal transfer of a phosphate group from C-3 to C-2 which results in the conversion of 3-phosphoglycerate (3PG) to 2-phosphoglycerate (2PG) through a 2,3-bisphosphoglycerate intermediate. These enzymes are categorized into the two distinct classes of either cofactor-dependent (dPGM) or cofactor-independent (iPGM). The dPGM enzyme is composed of approximately 250 amino acids and is found in all vertebrates as well as in some invertebrates, fungi, and bacteria. The iPGM class is found in all plants and algae as well as in some invertebrate, fungi, and Gram-positive bacteria. This class of PGM enzyme shares the same superfamily as alkaline phosphatase.
Amino acid synthesis is the set of biochemical processes by which the amino acids are produced. The substrates for these processes are various compounds in the organism's diet or growth media. Not all organisms are able to synthesize all amino acids. For example, humans can synthesize 11 of the 20 standard amino acids. These 11 are called the non-essential amino acids).
N-acetylglucosamine-1-phosphate transferase is a transferase enzyme.
In enzymology, a glycoprotein 2-beta-D-xylosyltransferase (EC 2.4.2.38) is an enzyme that catalyzes the chemical reaction
In enzymology, a glycoprotein 3-alpha-L-fucosyltransferase (EC 2.4.1.214) is an enzyme that catalyzes the chemical reaction
In enzymology, a glycoprotein 6-alpha-L-fucosyltransferase (EC 2.4.1.68) is an enzyme that catalyzes the chemical reaction
In enzymology, a mannosyl-3-phosphoglycerate synthase is an enzyme that catalyzes the chemical reaction
The haloacid dehydrogenase superfamily is a superfamily of enzymes that include phosphatases, phosphonatases, P-type ATPases, beta-phosphoglucomutases, phosphomannomutases, and dehalogenases, and are involved in a variety of cellular processes ranging from amino acid biosynthesis to detoxification.
Alpha-1,6-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase is an enzyme with systematic name UDP-N-acetyl-D-glucosamine:2,6-bis(N-acetyl-beta-D-glucosaminyl)-alpha-D-mannosyl-glycoprotein 4-beta-N-acetyl-D-glucosaminyltransferase. This enzyme catalyses the following chemical reaction
Mannosylglycerate synthase is an enzyme with systematic name GDP-mannose:D-glycerate 2-alpha-D-mannosyltransferase. This enzyme catalyses the following chemical reaction
Mannosylglucosyl-3-phosphoglycerate synthase is an enzyme with systematic name GDP-mannose:2-O-(alpha-D-glucosyl)-3-phospho-D-glycerate 2-O-alpha-D-mannosyltransferase. This enzyme catalyses the following chemical reaction
Glucosyl-3-phosphoglycerate phosphatase (EC 3.1.3.85, GpgP protein) is an enzyme with systematic name α-D-glucosyl-3-phospho-D-glycerate phosphohydrolase. This enzyme catalyses the following chemical reaction
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.
Mannosyl-oligosaccharide 1,2-α-mannosidase (EC 3.2.1.113, mannosidase 1A, mannosidase 1B, 1,2-α-mannosidase, exo-α-1,2-mannanase, mannose-9 processing α-mannosidase, glycoprotein processing mannosidase I, mannosidase I, Man9-mannosidase, ManI, 1,2-α-mannosyl-oligosaccharide α-D-mannohydrolase) is an enzyme with systematic name 2-α-mannosyl-oligosaccharide α-D-mannohydrolase. It catalyses the hydrolysis of the terminal (1→2)-linked α-D-mannose residues in the oligo-mannose oligosaccharide Man9(GlcNAc)2.
Mannosyl-oligosaccharide 1,3-1,6-α-mannosidase (EC 3.2.1.114, mannosidase II, exo-1,3-1,6-α-mannosidase, α-D-mannosidase II, α-mannosidase II, α-3,6-mannosidase, GlcNAc transferase I-dependent α1,3[α1,6]mannosidase, Golgi α-mannosidase II, ManII, 1,3(1,6)-α-D-mannosidase, 1,3-(1,6-)mannosyl-oligosaccharide α-D-mannohydrolase) is an enzyme with systematic name (1→3)-(1→6)-mannosyl-oligosaccharide α-D-mannohydrolase. It catalyses the hydrolysis of the terminal (1→3)- and (1→6)-linked α-D-mannose residues in the mannosyl-oligosaccharide Man5(GlcNAc)3.
Glycoprotein endo-α-1,2-mannosidase (EC 3.2.1.130, glucosylmannosidase, endo-α-D-mannosidase, endo-α-mannosidase, endomannosidase, glucosyl mannosidase) is an enzyme with systematic name glycoprotein glucosylmannohydrolase. It catalyses the hydrolysis of the terminal α-D-glucosyl-(1,3)-D-mannosyl unit from the GlcMan9(GlcNAc)2 oligosaccharide component of the glycoprotein produced in the Golgi membrane.
Mannosylglycerate hydrolase (EC 3.2.1.170, 2-O-(6-phospho-mannosyl)-D-glycerate hydrolase, alpha-mannosidase, mngB (gene)) is an enzyme with systematic name 2-O-(6-phospho-alpha-D-mannosyl)-D-glycerate acylhydrolase. This enzyme catalyses the following chemical reaction
References
- ↑ Empadinhas N, Marugg JD, Borges N, Santos H, da Costa MS (2001). "Pathway for the synthesis of mannosylglycerate in the hyperthermophilic archaeon Pyrococcus horikoshii. Biochemical and genetic characterization of key enzymes". J. Biol. Chem. 276 (47): 43580–8. doi: 10.1074/jbc.M108054200 . PMID 11562374.
