Information on EC 2.4.2.39 - xyloglucan 6-xylosyltransferase

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The expected taxonomic range for this enzyme is: rosids

EC NUMBER
COMMENTARY
2.4.2.39
-
RECOMMENDED NAME
GeneOntology No.
xyloglucan 6-xylosyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
hexosyl group transfer
-
-
-
-
hexosyl group transfer
-
xyloglucan alpha-(1,6)-xylosyltransferase activity, cell wall xyloglucan biosynthesis
PATHWAY
KEGG Link
MetaCyc Link
xyloglucan biosynthesis
-
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.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
At1g74380
Q9CA75
-
EC2.4.1.169
-
-
formerly
-
XXT5
Q9CA75
putative xyloglycan xylosylransferase
xyloglucan 6-alpha-D-xylosyltransferase
-
-
-
-
xyloglucan alpha-1,6-xylosyltransferase
O22775, Q9CA75, Q9LJP4, Q9LZJ3
-
xylosyltransferase, uridine diphosphoxylose-xyloglucan 6alpha-
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
80238-01-3
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
soy bean
-
-
Manually annotated by BRENDA team
dwarf-french-bean, cv. Canadian Wonder
-
-
Manually annotated by BRENDA team
pea, cv. Alaska or Caprice
-
-
Manually annotated by BRENDA team
tamarind
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
malfunction
Q9LJP4
double mutants for either xxt2 or xxt5 have a large impact on XyG content, structure and size distribution; double mutants for either xxt2 or xxt5 have a large impact on XyG content, structure and size distribution; overexpression of XXT3, is able to restore XyG epitopes in xxt2, xxt5 and xxt2 xxt5 double knockouts, suggesting that it also encodes a protein with XXT activity
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
UDP-D-xylose + (glucosyl)xyloglucan
UDP + (xylosyl-glucosyl)xyloglucan
show the reaction diagram
O22775, Q9LJP4, Q9LZJ3
-
-
-
?
UDP-D-xylose + (glucosyl)xyloglucan
UDP + (xylosyl-glucosyl)xyloglucan
show the reaction diagram
-, Q9CA75
-
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
show the reaction diagram
-
standard oligosaccharides for enzyme assay
-
-
?
UDP-D-xylose + (glucosyl)xyloglucan
UDP + (xylosyl-glucosyl)xyloglucan
show the reaction diagram
-
xylosyl-transfer is closely linked to glucosyl-transfer (EC 2.4.1.168)
-
?
UDP-D-xylose + (glucosyl)xyloglucan
UDP + (xylosyl-glucosyl)xyloglucan
show the reaction diagram
-
GDP-D-glucose or GDP-D-mannose cannot replace UDPxylose
-
?
UDP-D-xylose + (glucosyl)xyloglucan
UDP + (xylosyl-glucosyl)xyloglucan
show the reaction diagram
-
no acceptors are cello-oligosaccharides and fragment oligosaccharides from endoglucanase digest, other xylosyl-acceptors are beta-1,3-glucan and xylan
forms an alpha-1,6-D-xylosyl-D-glucose linkage
?
UDP-D-xylose + (glucosyl)xyloglucan
UDP + (xylosyl-glucosyl)xyloglucan
show the reaction diagram
-
transfers an alpha-D-xylosyl residue from UDP-D-xylose to a glucose residue in xyloglucan
-
?
UDP-D-xylose + (glucosyl)xyloglucan
UDP + (xylosyl-glucosyl)xyloglucan
show the reaction diagram
-
transfers an alpha-D-xylosyl residue from UDP-D-xylose to a glucose residue in xyloglucan
-
?
UDP-D-xylose + (glucosyl)xyloglucan
UDP + (xylosyl-glucosyl)xyloglucan
show the reaction diagram
-
transfers an alpha-D-xylosyl residue from UDP-D-xylose to a glucose residue in xyloglucan
-
?
UDP-D-xylose + (glucosyl)xyloglucan
UDP + (xylosyl-glucosyl)xyloglucan
show the reaction diagram
-
transfers an alpha-D-xylosyl residue from UDP-D-xylose to a glucose residue in xyloglucan
forms an alpha-1,6-D-xylosyl-D-glucose linkage
?
UDP-D-xylose + xyloglucan
?
show the reaction diagram
-
responsible for xyloglucan side-chain formation
-
-
?
UDP-D-xylose + xyloglucan
?
show the reaction diagram
-
involved in xyloglucan biosynthesis of higher plants
-
-
?
additional information
?
-
-, Q9CA75
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
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
UDP-D-xylose + (glucosyl)xyloglucan
UDP + (xylosyl-glucosyl)xyloglucan
show the reaction diagram
-, Q9CA75
-
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 + xyloglucan
?
show the reaction diagram
-
responsible for xyloglucan side-chain formation
-
-
?
UDP-D-xylose + xyloglucan
?
show the reaction diagram
-
involved in xyloglucan biosynthesis of higher plants
-
-
?
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ca2+
-
activation, can replace Mn2+ to some extent
Co2+
-
activation, can replace Mn2+ to some extent
Mg2+
-
activation, can replace Mn2+ to some extent
Mg2+
-
activation, can replace Mn2+ to some extent
Mn2+
-
10 mM; activation
Mn2+
-
activation
Mn2+
-
activation
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
Detergents
-
no solubilization possible due to this inhibition
Phosphate buffer
-
-
-
Tris-HCl buffer
-
-
GDPglucose
-
weak
additional information
-
no inhibition by tunicamycin, ATP or GTP
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
GDP-D-glucose
-
about half as effective as UDPglucose, in concentrations exceeding UDPxylose; activation
GDP-D-glucose
-
activation; protection
GDP-D-mannose
-
activation, protection
TDPglucose
-
activation, as effective as UDPglucose, in concentrations exceeding UDPxylose
UDPglucose
-
-
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
UDPglucose
-
2 mM
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
additional information
-
additional information
-
kinetic study
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
-
-
incorporation of xylosyl residues into polymeric acceptors
6.5
7
-
UDPglucose + UDPxylose
6.9
-
Q9LJP4
assay at; assay at; assay at; assay at
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
-
Q9LJP4
assay at; assay at; assay at; assay at
35
-
-
-
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
high expression level, revealed by Reverse Transcription-PCR
Manually annotated by BRENDA team
-
elongation region
Manually annotated by BRENDA team
-
expressed in all major organs, revealed by Reverse Transcription-PCR
Manually annotated by BRENDA team
-
high expression level, revealed by Reverse Transcription-PCR, shorter root hair and less root tissue xyloglucan detectable upon lack of XXT5
Manually annotated by BRENDA team
-
silique, lowest expression level, revealed by Reverse Transcription-PCR
Manually annotated by BRENDA team
-
high expression level, revealed by Reverse Transcription-PCR
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
immunolocalization of recombinant enzyme using tag-specific antibody, predicted Golgi-resident type-II membrane protein
Manually annotated by BRENDA team
-
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; 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; 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
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
51000
-
-
predicted from primary structure
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
heterodimer
-
existence of heterocomplexes XXT2-XXT5 and XXT1-XXT2 are demonstrated; existence of heterocomplexes XXT2-XXT5 and XXT5-CSLC4 are demonstrated; existence of heterocomplex XXT1-XXT2 is demonstrated
homodimer
-
existence of homocomplex XXT2-XXT2 is shown
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
DTT, 1 mM, EDTA, 1 mM, sucrose, 0.4 M, bovine serum albumin, 0.1%, stabilize
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
0°C, crude membrane-bound enzyme preparation, 1 day
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expressed in Escherichia coli as a truncated protein lacking the N-terminal transmembrane domain as GST-fusion protein; expressed in Escherichia coli as a truncated protein lacking the N-terminal transmembrane domain as GST-fusion protein; expressed in Escherichia coli as a truncated protein lacking the N-terminal transmembrane domain as GST-fusion protein; expressed in Escherichia coli as a truncated protein lacking the N-terminal transmembrane domain as GST-fusion protein
Q9LJP4
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
-