2.4.2.38: glycoprotein 2-beta-D-xylosyltransferase
This is an abbreviated version!
For detailed information about glycoprotein 2-beta-D-xylosyltransferase, go to the full flat file.
Word Map on EC 2.4.2.38
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2.4.2.38
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proteoglycans
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glycosaminoglycans
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desbuquois
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alpha1,3-fucosyltransferase
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laxity
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2.4.2.26
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udp-xylose
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chain-initiating
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xylosylated
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medicine
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alpha1,3-fucose
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biotechnology
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beta1,2-xylose
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o-xylosyltransferase
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synthesis
- 2.4.2.38
- proteoglycans
- glycosaminoglycans
-
desbuquois
-
alpha1,3-fucosyltransferase
-
laxity
-
2.4.2.26
- udp-xylose
-
chain-initiating
-
xylosylated
- medicine
-
alpha1,3-fucose
- biotechnology
-
beta1,2-xylose
-
o-xylosyltransferase
- synthesis
Reaction
Synonyms
beta 1,2-xylosyltransferase, beta-1,2-xylosyltransferase, beta-1,2-XylT, beta-1,4-mannosylglycoprotein beta-1,2-xylosyltransferase, beta1,2-xylosyltransferase, CAP3, Cryptococcal xylosyltransferase, cryptococcus xylosyltransferase 1, CXT1, Cxt1p, CXT1p homolog, RCN11, XT-I, XT1, Xt1p, Xyl-beta-1,2-transferase, xylan xylosyltransferase1, xylosyltransferase I, xylosyltransferase-I, XylT, XYLT1, XYXT1
ECTree
2.4.2.38 glycoprotein 2-beta-D-xylosyltransferaseAdvanced search results
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results (Engineering
Engineering on EC 2.4.2.38 - glycoprotein 2-beta-D-xylosyltransferase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
S53A
site-directed mutagenesis, possesses the N-glycosylation sites Asn301 and Asn478
T303A
site-directed mutagenesis, possesses the N-glycosylation sites Asn51 and Asn478
T480A
site-directed mutagenesis, possesses the N-glycosylation sites Asn51 and Asn301
D550A
mutation of first DXD motif to AXD, complete loss of activity, expression in Saccharomyces cerevisiae
D659A
mutation of second DXD motif to AXD, dramatic reduction in activity, expression in Saccharomyces cerevisiae
N141Q
mutation of the N-glycosylation site, molecular weight shift to 79 kDa corresponding to the molecular weight of the unmodified enzyme, no change in activity, expression in Saccharomyces cerevisiae
additional information
additional information
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construction of transgenic Nicotiana benthamiana plants expressing the CTSregion, T and C region, and a membrane-shed enzyme version, the latter is secreted to the apoplast, the T or C region constructs are located in the cytoplasm, the CTS construct is located in the cytoplasmic membrane, overview
additional information
serial deletions at both the N- and the C-terminal ends, integrity of a large domain located between amino acid 31 and the C-terminal lumenal region is required for activity, construction of transgenic tobacco expressing the enzyme via Agrobacterium tumefaciens infection system
additional information
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serial deletions at both the N- and the C-terminal ends, integrity of a large domain located between amino acid 31 and the C-terminal lumenal region is required for activity, construction of transgenic tobacco expressing the enzyme via Agrobacterium tumefaciens infection system
additional information
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construction of several N-terminal deletion mutants, the first 54 residues can be deleted without affecting the catalytic activity of the enzyme, removal of an additional five amino acids lead to the formation of an inactive protein
additional information
co-expression of human monoclonal antibodies with specific RNAi to block beta-1,2-xylosyltransferase and alpha-1,3-fucosyltransferase prevents unwanted plant specific N-glycosylation of the recombinant antibody proteins, method optimization, overview
additional information
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co-expression of human monoclonal antibodies with specific RNAi to block beta-1,2-xylosyltransferase and alpha-1,3-fucosyltransferase prevents unwanted plant specific N-glycosylation of the recombinant antibody proteins, method optimization, overview
additional information
targeted downregulation of the enzyme and the alpha1,3-fucosyltransferase allow production of heterologous proteins in a maize expression system
