Information on EC 2.4.1.B72 - C-mannosyltransferase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.4.1.B72
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RECOMMENDED NAME
GeneOntology No.
C-mannosyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
transfers a D-mannosyl residue from dolichyl D-mannosyl phosphate to the tryptophan residue of a protein acceptor forming a C-C bond
show the reaction diagram
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SYSTEMATIC NAME
IUBMB Comments
dolichyl-D-mannosyl-phosphate:protein C-mannosyltransferase
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene dpy-19
UniProt
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
DPY-19 exhibits topological and sequential homology to the N-glycan oligosaccharyltransferase, highlighting an evolutionary link between N- and C-glycosylation. The enzyme is related to the OST family involved in N-glycosylation
malfunction
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
dolichyl D-mannosyl phosphate + ADAMTS-like 1
dolichyl phosphate + C-mannosylated ADAMTS-like 1
show the reaction diagram
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purified recombinant tagged substrate. The substrate contains in thrombospondin type-1 repeats, two with predicted C-mannosylation sites, C-mannosylation of TSR1
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?
dolichyl D-mannosyl phosphate + human punctin-1
dolichyl phosphate + C-mannosylated human punctin-1
show the reaction diagram
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purified recombinant tagged substrate. C-mannosylation at Trp39 and Trp42 of a thrombospondin type-1 repeat containing the 36WDAWGPWSECSRTC49 sequence, identified by Tandem mass spectrometry (MS/MS) and MS/MS/MS analysis, TSR1 from punctin-1 carries C-mannosylation in close proximity to O-linked fucose
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?
dolichyl D-mannosyl phosphate + MIG-21 protein
dolichyl phosphate + C-mannosylated MIG-21 protein
show the reaction diagram
C-mannosylation at a tryptophan residue
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?
dolichyl D-mannosyl phosphate + UNC-5 protein
dolichyl phosphate + C-mannosylated UNC-5 protein
show the reaction diagram
C-mannosylation at a tryptophan residue
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?
dolichyl D-mannosyl phosphate + WAKW
dolichyl phosphate + ?
show the reaction diagram
in vitro assay using radiolabeled donor substrate and a synthetic acceptor peptide WAKW, which forms the minimal acceptor substrate
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?
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
dolichyl D-mannosyl phosphate + MIG-21 protein
dolichyl phosphate + C-mannosylated MIG-21 protein
show the reaction diagram
P34413
C-mannosylation at a tryptophan residue
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?
dolichyl D-mannosyl phosphate + UNC-5 protein
dolichyl phosphate + C-mannosylated UNC-5 protein
show the reaction diagram
P34413
C-mannosylation at a tryptophan residue
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?
additional information
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
transmembrane protein, membrane topology prediction and spacing between transmembrane domains of DPY-19, overview
Manually annotated by BRENDA team
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme, coexpressed with substrate Rspo1, by heparin and nickel affinity chromatography
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene dpy-19, recombinant expression in Drosophila melanogaster S2 cells, coexpression with receptor proteins UNC-5 or MIG-21
recombinant expression in S2 cells, coexpression with substrate Rspo1
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information