Mannosyl-oligosaccharide glucosidase

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Mannosyl-oligosaccharide glucosidase
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EC no. 3.2.1.106
CAS no. 78413-07-7
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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. [1] [2] [3] [4] [5] MOGS is a transmembrane protein found in the membrane of the endoplasmic reticulum of eukaryotic cells. Biologically, it functions within the N-glycosylation pathway.

Contents

Enzyme mechanism

MOGS is a glycoside hydrolase enzyme, belonging to Family 63 as classified within the Carbohydrate-Active Enzyme database. [6]

It catalyses exohydrolysis of the non-reducing terminal glucose residue in the mannosyl-oligosaccharide glycan Glc3Man9GlcNAc2.

This reaction is the first trimming step in the N-glycosylation pathway. Prior to this, the glycan was co-translationally attached to a nascent protein by the oligosaccharyltransferase complex. MOGS removes the terminal glucose residue, leaving the glycoprotein linked to Glc2Man9GlcNAc2, which can then serve as a substrate for glucosidase II.

The oligosaccharide substrate for MOGS MOGS substrate.png
The oligosaccharide substrate for MOGS

Substrate specificity

MOGS is highly specific to the oligosaccharide in its biological substrate in the N-glycosylation pathway. Eukaryotic MOGS does not cleave simple substrates such as p-nitrophenyl glucose, and it also shows no activity to the α(1→3) linkage present at the terminus of Glc1-2Man9GlcNAc2. [7] [8] [9] Furthermore, the minimum substrate is the glucotriose molecule (Glc-α(1→2)-Glc-α(1→3)-Glc), linked as in its native Glc3Man9GlcNAc2 substrate. Kojibiose, the disaccharide Glc-α(1→2)-Glc, acts as a weak inhibitor on plant, animal, and yeast MOGS. [8] [10] [11] [12]

MOGS also acts to lesser extent on the corresponding glycolipids and glycopeptides.

Related Research Articles

<span class="mw-page-title-main">Glycoprotein</span> Protein with oligosaccharide modifications

Glycoproteins are proteins which contain oligosaccharide (sugar) chains covalently attached to amino acid side-chains. The carbohydrate is attached to the protein in a cotranslational or posttranslational modification. This process is known as glycosylation. Secreted extracellular proteins are often glycosylated.

A congenital disorder of glycosylation is one of several rare inborn errors of metabolism in which glycosylation of a variety of tissue proteins and/or lipids is deficient or defective. Congenital disorders of glycosylation are sometimes known as CDG syndromes. They often cause serious, sometimes fatal, malfunction of several different organ systems in affected infants. The most common sub-type is PMM2-CDG where the genetic defect leads to the loss of phosphomannomutase 2 (PMM2), the enzyme responsible for the conversion of mannose-6-phosphate into mannose-1-phosphate.

<span class="mw-page-title-main">Oligosaccharyltransferase</span> Class of enzymes

Oligosaccharyltransferase or OST (EC 2.4.1.119) is a membrane protein complex that transfers a 14-sugar oligosaccharide from dolichol to nascent protein. It is a type of glycosyltransferase. The sugar Glc3Man9GlcNAc2 (where Glc=Glucose, Man=Mannose, and GlcNAc=N-acetylglucosamine) is attached to an asparagine (Asn) residue in the sequence Asn-X-Ser or Asn-X-Thr where X is any amino acid except proline. This sequence is called a glycosylation sequon. The reaction catalyzed by OST is the central step in the N-linked glycosylation pathway.

α-Glucosidase Enzyme

α-Glucosidase (EC 3.2.1.20, is a glucosidase located in the brush border of the small intestine that acts upon α bonds:

The enzyme mannosyl-glycoprotein endo-β-N-acetylglucosaminidase (endoglycosidase H) (EC 3.2.1.96) has systematic name glycopeptide-D-mannosyl-N4-(N-acetyl-D-glucosaminyl)2-asparagine 1,4-N-acetyl-β-glucosaminohydrolase. It is a highly specific endoglycosidase which cleaves asparagine-linked mannose rich oligosaccharides, but not highly processed complex oligosaccharides from glycoproteins. It is used for research purposes to deglycosylate glycoproteins and to monitor intracellular protein trafficking through the secretory pathway.

<span class="mw-page-title-main">GANC</span> Protein-coding gene in the species Homo sapiens

Neutral alpha-glucosidase C is an enzyme that in humans is encoded by the GANC gene.

<span class="mw-page-title-main">GCS1</span> Protein-coding gene in the species Homo sapiens

Mannosyl-oligosaccharide glucosidase is an enzyme that in humans is encoded by the MOGS gene.

<i>N</i>-linked glycosylation Attachment of an oligosaccharide to a nitrogen atom

N-linked glycosylation is the attachment of an oligosaccharide, a carbohydrate consisting of several sugar molecules, sometimes also referred to as glycan, to a nitrogen atom, in a process called N-glycosylation, studied in biochemistry. The resulting protein is called an N-linked glycan, or simply an N-glycan.

Alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase is an enzyme with systematic name UDP-N-acetyl-D-glucosamine:3-(alpha-D-mannosyl)-beta-D-mannosyl-glycoprotein 2-beta-N-acetyl-D-glucosaminyltransferase. This enzyme catalyses the following chemical reaction

Alpha-1,6-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase is an enzyme with systematic name UDP-N-acetyl-D-glucosamine:6-(alpha-D-mannosyl)-beta-D-mannosyl-glycoprotein 2-beta-N-acetyl-D-glucosaminyltransferase. This enzyme catalyses the following chemical reaction

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

GDP-Man:Man2GlcNAc2-PP-dolichol alpha-1,6-mannosyltransferase is an enzyme with systematic name GDP-D-mannose:D-Man-alpha-(1->3)-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol alpha-6-mannosyltransferase. This enzyme catalyses the following chemical reaction

Dolichyl-P-Man:Man5GlcNAc2-PP-dolichol alpha-1,3-mannosyltransferase is an enzyme with systematic name dolichyl beta-D-mannosyl phosphate:D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-(D-Man-alpha- )-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol alpha-1,3-mannosyltransferase. This enzyme catalyses the following chemical reaction

<span class="mw-page-title-main">ALG8 (enzyme class)</span> Class of enzymes

Dolichyl-P-Glc:Glc1Man9GlcNAc2-PP-dolichol alpha-1,3-glucosyltransferase is an enzyme with systematic name dolichyl beta-D-glucosyl phosphate:D-Glc-alpha-(1->3)-D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-(D-Man-alpha- -D-Man-alpha- - -D-Man-alpha- )-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol alpha-1,3-glucosyltransferase.

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, also known as Golgi α-mannosidase II, 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.

Mannosylglycoprotein endo-beta-mannosidase is an enzyme. This enzyme catalyses the following chemical reaction:

<span class="mw-page-title-main">PNGase F</span>

Peptide:N-glycosidase F, commonly referred to as PNGase F, is an amidase of the peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase class. PNGase F works by cleaving between the innermost GlcNAc and asparagine residues of high mannose, hybrid, and complex oligosaccharides from N-linked glycoproteins and glycopeptides. This results in a deaminated protein or peptide and a free glycan.

Armando J. Parodi is an Argentine glycobiologist. He did his initial education at the School of Sciences of the University of Buenos Aires. His PhD work was done under Luis Federico Leloir, a recipient of the Nobel Prize in Chemistry for his work involving the finding of sugar nucleotides and how they play a role in the making of oligosaccharides and polysaccharides. He also pursued postdoc work at the Pasteur Institute in Paris, France and Duke University in Durham, NC, USA.

References

  1. ↑ Elting JJ, Chen WW, Lennarz WJ (March 1980). "Characterization of a glucosidase involved in an initial step in the processing of oligosaccharide chains". The Journal of Biological Chemistry. 255 (6): 2325–31. PMID   7358674.
  2. ↑ Grinna LS, Robbins PW (September 1979). "Glycoprotein biosynthesis. Rat liver microsomal glucosidases which process oligosaccharides". The Journal of Biological Chemistry. 254 (18): 8814–8. PMID   479161.
  3. ↑ Kilker RD, Saunier B, Tkacz JS, Herscovics A (May 1981). "Partial purification from Saccharomyces cerevisiae of a soluble glucosidase which removes the terminal glucose from the oligosaccharide Glc3Man9GlcNAc2". The Journal of Biological Chemistry. 256 (10): 5299–603. PMID   7014569.
  4. ↑ Grinna LS, Robbins PW (March 1980). "Substrate specificities of rat liver microsomal glucosidases which process glycoproteins". The Journal of Biological Chemistry. 255 (6): 2255–8. PMID   7358666.
  5. ↑ Michael JM, Kornfeld S (January 1980). "Partial purification and characterization of the glucosidases involved in the processing of asparagine-linked oligosaccharides". Archives of Biochemistry and Biophysics. 199 (1): 249–58. doi:10.1016/0003-9861(80)90278-7. PMID   7356331.
  6. ↑ "CAZy - GH63". www.cazy.org. Retrieved 2016-04-05.
  7. ↑ Vijay IK, Shailubhai K, Dong-Yu B, Pratta MA, Saxena S (1988-04-01). "Studies on the biosynthesis and regulation of asparagine-linked glycoproteins in the lactating mammary gland". Indian Journal of Biochemistry & Biophysics. 25 (1–2): 127–32. PMID   2846425.
  8. 1 2 Dhanawansa R, Faridmoayer A, van der Merwe G, Li YX, Scaman CH (March 2002). "Overexpression, purification, and partial characterization of Saccharomyces cerevisiae processing α glucosidase I". Glycobiology. 12 (3): 229–34. doi:10.1016/0014-5793(86)80982-6. PMID   11971867.
  9. ↑ Shailubhai K, Saxena ES, Balapure AK, Vijay IK (June 1990). "Developmental regulation of glucosidase I, an enzyme involved in the processing of asparagine-linked glycoproteins in rat mammary gland". The Journal of Biological Chemistry. 265 (17): 9701–6. PMID   2190984.
  10. ↑ Zeng YC, Elbein AD (July 1998). "Purification to homogeneity and properties of plant glucosidase I". Archives of Biochemistry and Biophysics. 355 (1): 26–34. doi:10.1006/abbi.1998.0717. PMID   9647663.
  11. ↑ Schweden J, Borgmann C, Legler G, Bause E (July 1986). "Characterization of calf liver glucosidase I and its inhibition by basic sugar analogs". Archives of Biochemistry and Biophysics. 248 (1): 335–40. doi:10.1016/0003-9861(86)90429-7. PMID   2942110.
  12. ↑ Ugalde RA, Staneloni RJ, Leloir LF (December 1980). "Microsomal glucosidases of rat liver. Partial purification and inhibition by disaccharides". European Journal of Biochemistry. 113 (1): 97–103. doi: 10.1111/j.1432-1033.1980.tb06144.x . hdl: 11336/143170 . PMID   7460954.
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