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Information on EC 2.4.2.39 - xyloglucan 6-xylosyltransferase
for references in articles please use BRENDA:EC2.4.2.39
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EC Tree 2 Transferases
2.4 Glycosyltransferases
2.4.2 Pentosyltransferases
2.4.2.39 xyloglucan 6-xylosyltransferase
IUBMB Comments
In association with EC 2.4.1.168 (xyloglucan 4-glucosyltransferase), this enzyme brings about the synthesis of xyloglucan; concurrent transfers of glucose and xylose are necessary for this synthesis.
The enzyme appears in viruses and cellular organisms
Reaction Schemes
showSynonyms
xyloglucan alpha-1,6-xylosyltransferase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
EC 2.4.1.169
-
-
formerly
-
XXT1
XXT5
xyloglucan 6-alpha-D-xylosyltransferase
-
-
-
-
xyloglucan alpha-1,6-xylosyltransferase
xylosyltransferase, uridine diphosphoxylose-xyloglucan 6alpha-
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Transfers an alpha-D-xylosyl residue from UDP-D-xylose to a glucose residue in xyloglucan, forming an alpha-(1->6)-D-xylosyl-D-glucose linkage
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexosyl group transfer
hexosyl group transfer
-
-
-
-
hexosyl group transfer
xyloglucan alpha-(1,6)-xylosyltransferase activity, cell wall xyloglucan biosynthesis
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PATHWAY SOURCE
PATHWAYS
MetaCyc
xyloglucan biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
UDP-D-xylose:xyloglucan 6-alpha-D-xylosyltransferase
In association with EC 2.4.1.168 (xyloglucan 4-glucosyltransferase), this enzyme brings about the synthesis of xyloglucan; concurrent transfers of glucose and xylose are necessary for this synthesis.
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CAS REGISTRY NUMBER
COMMENTARY
80238-01-3
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
UDP-D-xylose + (glucosyl)xyloglucan
UDP + (xylosyl-glucosyl)xyloglucan
Substrates: -
Products: reduction of xyloglucan content (reduced glucan backbone substitution with xylose) in plants that lack functional XXT5 can be complemented by transformation with recombinant XXT5
Products: reduction of xyloglucan content (reduced glucan backbone substitution with xylose) in plants that lack functional XXT5 can be complemented by transformation with recombinant XXT5
?
UDP-D-xylose + (glucosyl)xyloglucan
UDP + (xylosyl-glucosyl)xyloglucan
Substrates: -
Products: -
Products: -
?
UDP-D-xylose + (glucosyl)xyloglucan
UDP + (xylosyl-glucosyl)xyloglucan
-
Substrates: xylosyl-transfer is closely linked to glucosyl-transfer (EC 2.4.1.168)
Products: -
Products: -
?
UDP-D-xylose + (glucosyl)xyloglucan
UDP + (xylosyl-glucosyl)xyloglucan
-
Substrates: no acceptors are cello-oligosaccharides and fragment oligosaccharides from endoglucanase digest
Products: forms an alpha-1,6-D-xylosyl-D-glucose linkage
Products: forms an alpha-1,6-D-xylosyl-D-glucose linkage
?
UDP-D-xylose + (glucosyl)xyloglucan
UDP + (xylosyl-glucosyl)xyloglucan
-
Substrates: other xylosyl-acceptors are beta-1,3-glucan and xylan
Products: forms an alpha-1,6-D-xylosyl-D-glucose linkage
Products: forms an alpha-1,6-D-xylosyl-D-glucose linkage
?
UDP-D-xylose + (glucosyl)xyloglucan
UDP + (xylosyl-glucosyl)xyloglucan
-
Substrates: transfers an alpha-D-xylosyl residue from UDP-D-xylose to a glucose residue in xyloglucan
Products: -
Products: -
?
UDP-D-xylose + (glucosyl)xyloglucan
UDP + (xylosyl-glucosyl)xyloglucan
-
Substrates: transfers an alpha-D-xylosyl residue from UDP-D-xylose to a glucose residue in xyloglucan
Products: forms an alpha-1,6-D-xylosyl-D-glucose linkage
Products: forms an alpha-1,6-D-xylosyl-D-glucose linkage
?
UDP-D-xylose + (glucosyl)xyloglucan
UDP + (xylosyl-glucosyl)xyloglucan
-
Substrates: transfers an alpha-D-xylosyl residue from UDP-D-xylose to a glucose residue in xyloglucan
Products: -
Products: -
?
UDP-D-xylose + (glucosyl)xyloglucan
UDP + (xylosyl-glucosyl)xyloglucan
-
Substrates: -
Products: -
Products: -
?
UDP-D-xylose + (glucosyl)xyloglucan
UDP + (xylosyl-glucosyl)xyloglucan
-
Substrates: GDP-D-glucose or GDP-D-mannose cannot replace UDPxylose
Products: -
Products: -
?
UDP-D-xylose + (glucosyl)xyloglucan
UDP + (xylosyl-glucosyl)xyloglucan
-
Substrates: standard oligosaccharides for enzyme assay
Products: -
Products: -
?
UDP-D-xylose + xyloglucan
?
-
Substrates: responsible for xyloglucan side-chain formation
Products: -
Products: -
?
UDP-D-xylose + xyloglucan
?
-
Substrates: involved in xyloglucan biosynthesis of higher plants
Products: -
Products: -
?
additional information
?
-
Substrates: no xylosyltransferase activity in vitro after expression in either Pichia pastoris or Sf21 insect cells using UDP-xylose and a broad range of putative acceptors
Products: -
Products: -
?
additional information
?
-
-
Substrates: no xylosyltransferase activity in vitro after expression in either Pichia pastoris or Sf21 insect cells using UDP-xylose and a broad range of putative acceptors
Products: -
Products: -
?
additional information
?
-
-
Substrates: there is an association of the enzyme and water-extractable arabinoxylan
Products: -
Products: -
-
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
UDP-D-xylose + (glucosyl)xyloglucan
UDP + (xylosyl-glucosyl)xyloglucan
Substrates: -
Products: reduction of xyloglucan content (reduced glucan backbone substitution with xylose) in plants that lack functional XXT5 can be complemented by transformation with recombinant XXT5
Products: reduction of xyloglucan content (reduced glucan backbone substitution with xylose) in plants that lack functional XXT5 can be complemented by transformation with recombinant XXT5
?
UDP-D-xylose + (glucosyl)xyloglucan
UDP + (xylosyl-glucosyl)xyloglucan
-
Substrates: -
Products: -
Products: -
?
UDP-D-xylose + xyloglucan
?
-
Substrates: responsible for xyloglucan side-chain formation
Products: -
Products: -
?
UDP-D-xylose + xyloglucan
?
-
Substrates: involved in xyloglucan biosynthesis of higher plants
Products: -
Products: -
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mn2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TDPglucose
-
activation, as effective as UDPglucose, in concentrations exceeding UDPxylose
GDP-D-glucose
-
about half as effective as UDPglucose, in concentrations exceeding UDPxylose
UDPglucose
-
activation, xylose is effectively incorporated in the presence of UDPglucose, the transfer must be preceded by elongation of the beta-1,4-glucan-backbone, because xylosyl residues constitute the side chains, in concentrations exceeding UDPxylose, no activation by CDPglucose or ADPglucose
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
high expression level, revealed by Reverse Transcription-PCR
brenda
expressed in all major organs, revealed by Reverse Transcription-PCR
brenda
high expression level, revealed by Reverse Transcription-PCR, shorter root hair and less root tissue xyloglucan detectable upon lack of XXT5
brenda
silique, lowest expression level, revealed by Reverse Transcription-PCR
brenda
high expression level, revealed by Reverse Transcription-PCR
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
immunolocalization of recombinant enzyme using tag-specific antibody, predicted Golgi-resident type-II membrane protein
brenda
complex formation in vivo and potential physical interactions among three xylosyltransferases, XXT1, XXT2, and XXT5, and a glucan synthase, CSLC4 is shown in the Golgi membrane in Arabidopsis cells
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
-
the enzyme maintains cell wall structure and tensile strength in rice
malfunction
double mutants for either xxt2 or xxt5 have a large impact on XyG content, structure and size distribution
Show AA Sequence and Transmembrane Helices (1091 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
heterodimer
homodimer
existence of homocomplex XXT2-XXT2 is shown
heterodimer
existence of heterocomplexes XXT2-XXT5 and XXT1-XXT2 are demonstrated
heterodimer
existence of heterocomplex XXT1-XXT2 is demonstrated
heterodimer
existence of heterocomplexes XXT2-XXT5 and XXT5-CSLC4 are demonstrated
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli as a truncated protein lacking the N-terminal transmembrane domain as GST-fusion protein
in pENTR/D-TOPO downstream of cauliflower mosaic virus 35S promoter for recombination with pEarleyGate 201 and Agrobacterium tumefacies strain GV3101-mediated transformation (floral-flip), expression with hemagglutinin (HA) tag
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hayashi, T.; Koyama, T.; Matsuda, K.
Formation of UDP-xylose and xyloglucan in soybean Golgi membranes
Plant Physiol.
87
341-345
1988
Glycine max
brenda
Hayashi, T.; Matsuda, K.
Biosynthesis of xyloglucan in suspension-cultured soybean cells. Occurrence and some properties of xyloglucan 4-beta-D-glucosyltransferase and 6-alpha-D-xylosyltransferase
J. Biol. Chem.
256
11117-11122
1981
Glycine max
brenda
White, A.R.; Xin, Y.; Pezeshk, V.
Xyloglucan glucosyltransferase in Golgi membranes from Pisum sativum (pea)
Biochem. J.
294
231-238
1993
Lathyrus oleraceus
brenda
Hayashi, T.; Matsuda, K.
Biosynthesis of xyloglucan in suspension-cultured soybean cells. Evidence that the enzyme system of xyloglucan synthesis does not contain beta-1,4-glucan 4-beta-glucosyltransferase activity (EC 2.4.1.12)
Plant Cell Physiol.
22
1571-1584
1981
Glycine max
-
brenda
Marry, M.; Cavalier, D.M.; Schnurr, J.K.; Netland, J.; Yang, Z.; Pezeshk, V.; York, W.S.; Pauly, M.; White, A.R.
Structural characterization of chemically and enzymatically derived standard oligosaccharides isolated from partially purified tamarind xyloglucan
Carbohydr. Polym.
51
347-356
2002
Tamarindus indica
-
brenda
Campbell, R.E.; Brett, C.T.; Hillman, J.R.
A xylosyltransferase involved in the synthesis of a protein-associated xyloglucan in suspension-cultured dwarf-French-bean (Phaseolus vulgaris) cells and its interaction with a glucosyltransferase
Biochem. J.
253
795-800
1988
Phaseolus vulgaris
brenda
Zabotina, O.A.; van de Ven, W.T.; Freshour, G.; Drakakaki, G.; Cavalier, D.; Mouille, G.; Hahn, M.G.; Keegstra, K.; Raikhel, N.V.
Arabidopsis XXT5 gene encodes a putative alpha-1,6-xylosyltransferase that is involved in xyloglucan biosynthesis
Plant J.
56
101-115
2008
Arabidopsis thaliana (Q9CA75), Arabidopsis thaliana
brenda
Vuttipongchaikij, S.; Brocklehurst, D.; Steele-King, C.; Ashford, D.A.; Gomez, L.D.; McQueen-Mason, S.J.
Arabidopsis GT34 family contains five xyloglucan alpha-1,6-xylosyltransferases
New Phytol.
195
585-595
2012
Arabidopsis thaliana (Q9CA75), Arabidopsis thaliana (Q9LZJ3), Arabidopsis thaliana (O22775), Arabidopsis thaliana (Q9LJP4)
brenda
Chou, Y.H.; Pogorelko, G.; Zabotina, O.A.
Xyloglucan xylosyltransferases XXT1, XXT2, and XXT5 and the glucan synthase CSLC4 form Golgi-localized multiprotein complexes
Plant Physiol.
159
1355-1366
2012
Arabidopsis thaliana (Q9CA75), Arabidopsis thaliana (Q9LZJ3), Arabidopsis thaliana (O22775)
brenda
Wang, C.; Li, S.; Ng, S.; Zhang, B.; Zhou, Y.; Whelan, J.; Wu, P.; Shou, H.
Mutation in xyloglucan 6-xylosytransferase results in abnormal root hair development in Oryza sativa
J. Exp. Bot.
65
4149-4157
2014
Oryza sativa
brenda
Siekmann, D.; Jansen, G.; Zaar, A.; Kilian, A.; Fromme, F.J.; Hackauf, B.
A genome-wide association study pinpoints quantitative trait genes for plant height, heading date, grain quality, and yield in rye (Secale cereale L.)
Front. Plant Sci.
12
718081
2021
Secale cereale
brenda
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