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Information on EC 2.4.1.B3 - alpha-1,4-glucan synthase Word Map on EC 2.4.1.B3
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The enzyme appears in viruses and cellular organisms
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2.4.1.B3
preliminary BRENDA-supplied EC number
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alpha-1,4-glucan synthase
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UDP-glucose + [alpha-D-glucosyl-(1-3)]n = UDP + alpha-1,4-glucosyl-[alpha-D-glucosyl-(1-3)]n
UDP-glucose + [alpha-D-glucosyl-(1-3)]n = UDP + alpha-1,4-glucosyl-[alpha-D-glucosyl-(1-3)]n
adds the approximately 10% of alpha-1,4-linked glucose residues to alpha-1,3-glucan chains
UDP-glucose + [alpha-D-glucosyl-(1-3)]n = UDP + alpha-1,4-glucosyl-[alpha-D-glucosyl-(1-3)]n
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UDP-glucose:alpha-D-(1-3)-glucan alpha-(1-4)-glucosyltransferase
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Ags1p
multidomain protein with two probable catalytic domains predicted to reside at opposite sides of the plasma membrane, as well as a multipass transmembrane domain
cell wall alpha-1,4-glucan synthase
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UniProt
brenda
study deals with the intracellular domain of the protein
UniProt
brenda
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additional information
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additional information
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alpha-1,3-glucan, synthesized by the enzyme Ags1p, is essentially a linear polysaccharide, with 3% of alpha-1,4-linked glucose branches, occasionally attached as single units to the alpha-1,3-backbone
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additional information
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required for the biosynthesis of alpha-1,4-glucan in cell wall alpha-glucan
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additional information
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required for the biosynthesis of alpha-1,4-glucan in cell wall alpha-glucan
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additional information
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additional information
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Q9USK8
required for the biosynthesis of alpha-1,4-glucan in cell wall alpha-glucan
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additional information
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required for the biosynthesis of alpha-1,4-glucan in cell wall alpha-glucan
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brenda
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265000
x * 265000, SDS-PAGE
272106
x * 272106, calculated from the deduced amino acid sequence
274335
x * 274335, calculated
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x * 274335, calculated
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x * 265000, SDS-PAGE; x * 272106, calculated from the deduced amino acid sequence
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expression of native and E1526A mutant enzyme in Schizosaccharomyces pombe, overexpression of native but not mutant enzyme results in accumulation of (1,4)-alpha-glucan
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mRNAs levels of Ras homology GTPase RHO2 and enzyme gene AGS1 keep a direct relationship but the levels of Ras homology GTPase RHO1 and beta-1,3-glucan synthase FKS1 do not. Growth of cells in the Y phase in YPG medium supplemented with 5% horse serum leads to an increase in the alpha-1,3-glucan content of the cell wall, without signifi cant increase in AGS1 expression, regardless of the Y cells being grown in the presence or absence of horse serum
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DELTA1118-1689
enzyme is not able to synthesize alpha-1,4-glucan
DELTA113-724
enzyme is able to synthesize alpha-1,4-glucan
E1526A
markedly reduced ability to complement the cell lysis phenotype and temperature sensitivity of the Schizosaccharomyces pombe ags1-1 mutant, no accumulation of alpha-1,4-glucan
E1534A
able to complement the cell lysis phenotype and temperature sensitivity of the Schizosaccharomyces pombe ags1-1 mutant
G1165A
able to complement the cell lysis phenotype and temperature sensitivity of the Schizosaccharomyces pombe ags1-1 mutant
G696S
temperature-sensitive mutation, gene is functional at 28°C but not at 36°C
K1163Q
able to complement the cell lysis phenotype and temperature sensitivity of the Schizosaccharomyces pombe ags1-1 mutant
K1422Q
reduced accumulation of alpha-1,4-glucan
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Q5S3X6_PARBR
2431
274336
TrEMBL
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Vos, A.; Dekker, N.; Distel, B.; Leunissen, J.A.; Hochstenbach, F.
Role of the synthase domain of Ags1p in cell wall alpha-glucan biosynthesis in fission yeast
J. Biol. Chem.
282
18969-18979
2007
Schizosaccharomyces pombe (Q9USK8), Schizosaccharomyces pombe
brenda
Sorais, F.; Barreto, L.; Leal, J.; Bernabe, M.; San-Blas, G.; Nino-Vega, G.
Cell wall glucan synthases and GTPases in Paracoccidioides brasiliensis
Med. Mycol.
48
35-47
2010
Paracoccidioides brasiliensis, Paracoccidioides brasiliensis (Q5S3X6)
brenda
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