2.4.1.132: GDP-Man:Man1GlcNAc2-PP-dolichol alpha-1,3-mannosyltransferase
This is an abbreviated version!
For detailed information about GDP-Man:Man1GlcNAc2-PP-dolichol alpha-1,3-mannosyltransferase, go to the full flat file.
Word Map on EC 2.4.1.132
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2.4.1.132
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alpha-1,2-mannosyltransferase
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lipid-linked
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alpha-1,3-linked
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mannoses
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beta-glcnac
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oligosaccharide-lipids
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mannans
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pharmacology
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medicine
- 2.4.1.132
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alpha-1,2-mannosyltransferase
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lipid-linked
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alpha-1,3-linked
- mannoses
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beta-glcnac
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oligosaccharide-lipids
- mannans
- pharmacology
- medicine
Reaction
Synonyms
Alg2, Alg2 mannosyltransferase, Alg2 MTase, alpha-1,3-mannosyltransferase, alpha-1,3-ManT, asparagine-linked glycosylation 2, GDP-Man:Dol-PP-GlcNAc2Man2 alpha-1,3-mannosyltransferase, GDP-Man:Man1GlcNAc2-PP-dolichol mannosyltransferase, GDP-mannose-oligosaccharide-lipid mannosyltransferase II, hALG2, mannosyltransferase II, mannosyltransferase, guanosine diphosphomannose-oligosaccharide-lipid II, More, MTase, scAlg2, WfcD
ECTree
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Engineering
Engineering on EC 2.4.1.132 - GDP-Man:Man1GlcNAc2-PP-dolichol alpha-1,3-mannosyltransferase
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G393T/DELTAG1040
mutation in a patient with a congenital disorders of glycosylation designated CDG-Ii caused by ALG2 deficiency
V68G
E335A
E335A/E343A
significant lower level of product formation, identical to that of the E335A mutant
E343A
F337A
site-directed mutagenesis, Trx-scAlg2F337A produces 26% Man3Gn2 product compared to wild-type enzyme
G377R
site-directed mutagenesis, a temperature-sensitive alg2-1 mutant containing a single missense mutation, catalytically inactive
H336A
V62G
site-directed mutagenesis, Trx-scAlg2V62G produces 25% Man3Gn2 product compared to wild-type enzyme. The HA-tagged mutant allele (3HAscAlg2V62G) fails to complement the lethality of the alg2DELTA LSY2 when grown on 5-FOA
E335A
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site-directed mutagenesis, Trx-scAlg2E335A produces only no final product and only 32% of intermediate Man2Gn2 compared to wild-type enzyme
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F337A
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site-directed mutagenesis, Trx-scAlg2F337A produces 26% Man3Gn2 product compared to wild-type enzyme
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H336A
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site-directed mutagenesis, Trx-scAlg2H336A produces 8% Man3Gn2 product compared to wild-type enzyme
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additional information
naturally occuring mutation, a non-conservative change, a pathogenic mutation causing a rare congenital disorder such as congenital myasthenic syndrome, CMS
V68G
site-directed mutagenesis, the mutant shows reduced expression in muscle
E335A
site-directed mutagenesis, Trx-scAlg2E335A produces only no final product and only 32% of intermediate Man2Gn2 compared to wild-type enzyme
H336A
site-directed mutagenesis, Trx-scAlg2H336A produces 8% Man3Gn2 product compared to wild-type enzyme
additional information
variant c.214_226delinsAGTCCCCGGC, p.72_75delinsSPR, removes a highly conserved GDWL motif of the glycosyltransferase 4-like domain, and inserts three different amino acids
additional information
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variant c.214_226delinsAGTCCCCGGC, p.72_75delinsSPR, removes a highly conserved GDWL motif of the glycosyltransferase 4-like domain, and inserts three different amino acids
additional information
ALG2 downregulation in ST-2 cells by siRNA transfection
additional information
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ALG2 downregulation in ST-2 cells by siRNA transfection
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additional information
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ALG2 mutant with severely reduced enzyme activity
additional information
ALG2 mutant with severely reduced enzyme activity
additional information
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mutagenesis of Mnn1p by altering either of the 2 conserved aspartates eliminates all enzymic activity, but does not affect the overall folding and assembly of Mnn1p
additional information
mutational analysis of Alg2 and identification of amino acids required for its activity. None of the four domains (predicted as transmembrane-spanning helices) is essential for transferase activity because truncated Alg2 variants can exert their function as long as Alg2 is associated with the endaplasmic reticulum by either its N- or C-terminal hydrophobic regions
additional information
site-directed mutagenesis of conserved EX7E motif. Trx-scAlg2E335A, mutated in the first E, has significantly decreased activity, producing no final product and only 32% of intermediate Man2Gn2. Trx-scAlg2E343A, mutated in the second E, has no detectable activity. The intervening amino acids of the EX7E are also important, though less than either E335 or E343. Trx-scAlg2H336A and Trx-scAlg2F337A produce 8% and 26% of Man3Gn2 product, respectively, compared to wild-type. Cells deleted for ALG2 are inviable, a plasmid shuffling technique is used to measure complementation. Mutant alg2 alleles display intraallelic complementation. Mutations (changed to proline) in five of the glycines (G19, G20, G256, G357, G358) result in complete loss of activity, while two of them (G17, G257) are significantly decreased
additional information
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ALG2 mutant with severely reduced enzyme activity
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additional information
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mutagenesis of Mnn1p by altering either of the 2 conserved aspartates eliminates all enzymic activity, but does not affect the overall folding and assembly of Mnn1p
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additional information
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site-directed mutagenesis of conserved EX7E motif. Trx-scAlg2E335A, mutated in the first E, has significantly decreased activity, producing no final product and only 32% of intermediate Man2Gn2. Trx-scAlg2E343A, mutated in the second E, has no detectable activity. The intervening amino acids of the EX7E are also important, though less than either E335 or E343. Trx-scAlg2H336A and Trx-scAlg2F337A produce 8% and 26% of Man3Gn2 product, respectively, compared to wild-type. Cells deleted for ALG2 are inviable, a plasmid shuffling technique is used to measure complementation. Mutant alg2 alleles display intraallelic complementation. Mutations (changed to proline) in five of the glycines (G19, G20, G256, G357, G358) result in complete loss of activity, while two of them (G17, G257) are significantly decreased
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