2.4.1.109: dolichyl-phosphate-mannose-protein mannosyltransferase
This is an abbreviated version!
For detailed information about dolichyl-phosphate-mannose-protein mannosyltransferase, go to the full flat file.
Word Map on EC 2.4.1.109
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2.4.1.109
-
muscular
-
dystrophy
-
o-mannosylation
-
walker-warburg
-
alpha-dystroglycan
-
pomgnt1
-
o-glycosylation
-
fukutin
-
muscle-eye-brain
-
dystroglycanopathies
-
dystroglycan
-
girdle
-
alpha-dystroglycanopathy
-
lissencephaly
-
fukuyama
-
hypoglycosylation
-
limb-girdle
-
alpha-dg
-
pomts
-
cobblestone
-
heterotopia
-
fukutin-related
-
medicine
-
gmppb
-
o-mannose
-
agriculture
-
diagnostics
- 2.4.1.109
- muscular
- dystrophy
-
o-mannosylation
-
walker-warburg
- alpha-dystroglycan
- pomgnt1
-
o-glycosylation
-
fukutin
- muscle-eye-brain
- dystroglycanopathies
-
dystroglycan
-
girdle
-
alpha-dystroglycanopathy
- lissencephaly
-
fukuyama
-
hypoglycosylation
-
limb-girdle
-
alpha-dg
-
pomts
-
cobblestone
- heterotopia
-
fukutin-related
- medicine
- gmppb
-
o-mannose
- agriculture
- diagnostics
Reaction
Synonyms
AapmtA, AfPmt1p, AnPmtA, AnPmtB, AnPmtC, dolichol phosphomannose-protein mannosyltransferase, dolichyl phosphate-mannose:protein O-mannosyltransferase, dolichyl-phosphate-mannose--protein mannosyltransferase 1, dolichyl-phosphate-mannose--protein mannosyltransferase 2, dolichyl-phosphate-mannose--protein mannosyltransferase 4, dolichyl-phosphate-mannose-protein mannosyltransferase, dolichyl-phosphate-mannose-protein mannosyltransferase 1, dolichyl-phosphate-mannose-protein mannosyltransferase 2, Drosophila O-mannosyltransferase Rotated Abdomen, Drosophila O-mannosyltransferase Twisted, HpPmt1p, mannosyltransferase, dolichol phosphomannose-protein, More, O-glycoside mannosyltransferase, O-mannosyltransferase, O-mannosyltransferase 1, ogm1, ogm2, ogm4, Oma1, Oma2, Oma4, Omg1, Omg2, Omg4, PMT, PMT1, Pmt1 O-mannosyltransferase, Pmt1A, Pmt1D, Pmt1p, Pmt1p-Pmt2p, PMT2, Pmt2A, Pmt2D, Pmt2p, PMT3, PMT4, Pmt4A, Pmt4D, Pmt4p, PMT5, Pmt5p, Pmt6, PMT7, PmtA, pmtB, pmtC, PMTI, POMT1, POMT2, protein mannosyltransferase, protein O-D-mannosyltransferase, protein O-mannosyl-transferase 1, protein O-mannosyl-transferase 2, protein O-mannosyltransferase, protein O-mannosyltransferase 1, protein O-mannosyltransferase 2, protein O-mannosyltransferase A, protein O-mannosyltransferase Pmt4, protein O-mannosyltransferases 1, protein O-mannosyltransferases 2, protein-O-mannosyltransferase-1, protein-Omannosyltransferase, RT, sPOMT2, tPOmt2, TW, Um05433, Um10749, Um11220
ECTree
2.4.1.109 dolichyl-phosphate-mannose-protein mannosyltransferaseAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 2.4.1.109 - dolichyl-phosphate-mannose-protein mannosyltransferase
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
dolichyl beta-D-mannosyl phosphate + L-seryl-[protein]
dolichyl phosphate + 3-O-(alpha-D-mannosyl)-L-seryl-[protein]
dolichyl beta-D-mannosyl phosphate + L-threonyl-[protein]
dolichyl phosphate + 3-O-(alpha-D-mannosyl)-L-threonyl-[protein]
dolichyl beta-D-mannosyl phosphate + synthetic peptide based on a mucin-like domain in alpha-dystroglycan
?
-
-
-
-
?
dolichyl D-mannosyl phosphate + YATAVK-Btn
dolichyl phosphate + O-D-mannosyl-YATAVK-Btn
photocross-linking reaction based on the peptide YATAVK-Btn that serves as in vitro mannosyl acceptor substrate of Pmt1p/Pmt2p and is O -mannosylated to a similar extent as the known acceptor peptide AcNH-YATAV-CONH2
-
-
?
dolichyl phosphate D-mannose + Ac-Ala-Thr-Ala-NH2
dolichyl phosphate + O-D-mannosyl-Ac-Ala-Thr-Ala-NH2
-
-
-
?
dolichyl phosphate D-mannose + Ac-Tyr-Ala-Thr-Ala-Val-NH2
dolichyl phosphate + O-D-mannosyl-Ac-Tyr-Ala-Thr-Ala-Val-NH2
dolichyl phosphate D-mannose + Ac-Tyr-Asn-Pro-Thr-Ser-Val-NH2
dolichyl phosphate + O-D-mannosyl-Ac-Tyr-Asn-Pro-Thr-Ser-Val-NH2
dolichyl phosphate D-mannose + alpha-dystroglycan
dolichyl phosphate + O-D-mannosyl-[alpha-dystroglycan]
-
in vitro asssay with both enzyme isoforms (RT and TW), 20 mM Tris, pH 8.0, mercaptoethanol, EDTA, n-octyl-beta-D-thioglucoside, sugar donor is tritium-labeled, alpha-dystroglycan isoform C contains mucin-type domain that is target of O-mannose modifications in mammals, high grade of O-mannosylation, A isoform without noticeable O-mannosylation, rabbit alpha-dystroglycan as positive control shows lower O-mannosylation
-
-
?
dolichyl phosphate D-mannose + alpha-dystroglycan glutathione-S-transferase fusion protein
dolichyl phosphate + O-D-mannosyl-[alpha-dystroglycan]
sugar donor tritium-labeled
-
-
?
dolichyl phosphate D-mannose + Asn-Ala-Thr-Val-dinitrophenyl
dolichyl phosphate + O-D-mannosyl-Asn-Ala-Thr-Val-dinitrophenyl
-
-
-
?
dolichyl phosphate D-mannose + biotin-Tyr-Ala-Thr-Ala-Val-NH2
dolichyl phosphate + O-D-mannosyl-N-biotinyl-Tyr-Ala-Thr-Ala-Val-NH2
dolichyl phosphate D-mannose + biotin-Tyr-Pro-Thr-Ala-Val-NH2
dolichyl phosphate + O-D-mannosyl-N-biotinyl-Tyr-Pro-Thr-Ala-Val-NH2
-
-
-
?
dolichyl phosphate D-mannose + biotin-Tyr-Thr-Ala-Val-NH2
dolichyl phosphate + O-D-mannosyl-N-biotinyl-Tyr-Thr-Ala-Val-NH2
-
-
-
?
dolichyl phosphate D-mannose + Gas1p
dolichyl phosphate + O-D-mannosyl-Gas1p
-
-
-
-
?
dolichyl phosphate D-mannose + glucoamylase I
dolichyl phosphate + O-D-mannosyl glucoamylase I
dolichyl phosphate D-mannose + glucoamylase I
dolichyl phosphate + O-D-mannosyl-[glucoamylase]
-
extracellular Aspergillus awamori protein as reporter for glycosylation measurements, underglycosylation upon AnpmtA, AnpmtB, and AnpmtC diruption
-
-
?
dolichyl phosphate D-mannose + glutathione-S-transferase fusion alpha-dystroglycan
dolichyl phosphate + O-D-mannosyl-glutathione-S-transferase fusion alpha-dystroglycan
dolichyl phosphate D-mannose + glutathione-S-transferase fusion alpha-dystroglycan
dolichyl phosphate + O-D-mannosyl-[alpha-dystroglycan]
-
tritium-labeled sugar donor, 20 mM Tris-HCl, pH 8.0, 2-mercaptoethanol, EDTA, n-octyl-beta-D-thiogucoside, 22°C
-
-
?
dolichyl phosphate D-mannose + glutathione-S-transferase fusion alpha-dystroglycan
dolichyl phosphate + O-D-mannosyl-[glutathione-S-transferase fusion alpha-dystroglycan]
-
-
-
-
?
dolichyl phosphate D-mannose + human ribonuclease 2
dolichyl phosphate + human ribonuclease 2-D-mannose
dolichyl phosphate D-mannose + Lys-Pro-Ser-Gly-Tyr
dolichyl phosphate + O-D-mannosyl-Lys-Pro-Ser-Gly-Tyr
-
-
-
?
dolichyl phosphate D-mannose + Lys-Pro-Thr-Gly-Tyr
dolichyl phosphate + O-D-mannosyl-Lys-Pro-Thr-Gly-Tyr
-
-
-
?
dolichyl phosphate D-mannose + Lys-Pro-Thr-Pro-Tyr
dolichyl phosphate + O-D-mannosyl-Lys-Pro-Thr-Pro-Tyr
-
-
-
?
dolichyl phosphate D-mannose + N-acetyl-SSSSS
dolichyl phosphate + O-D-mannosyl-N-acetyl-SSSSS
-
worst substrate
-
-
?
dolichyl phosphate D-mannose + N-acetyl-YASAV
dolichyl phosphate + O-D-mannosyl-N-acetyl-YASAV
-
-
-
-
?
dolichyl phosphate D-mannose + N-acetyl-YATAV
dolichyl phosphate + O-D-mannosyl-N-acetyl-YATAV
-
best substrate
-
-
?
dolichyl phosphate D-mannose + N-acetyl-YATAVK-biotin
dolichyl phosphate + O-D-mannosyl-N-acetyl-YATAVK-biotin
-
N-acetyl-YATAVK-biotin preferentially reacts with isoform Pmt1p
-
-
?
dolichyl phosphate D-mannose + Pro-Thr-Val
dolichyl phosphate + O-D-mannosyl-Pro-Thr-Val
-
-
-
?
dolichyl phosphate D-mannose + Pro-Tyr-Thr-Val
dolichyl phosphate + O-D-mannosyl-Pro-Tyr-Thr-Val
-
-
-
?
dolichyl phosphate D-mannose + protein chitinase 1
dolichyl phosphate + O-D-mannosylprotein chitinase 1
dolichyl phosphate D-mannose + protein Ggp1/Gas1
dolichyl phosphate + O-D-mannosylprotein Ggp1/Gas1
dolichyl phosphate D-mannose + protein Pir2/hsp150
dolichyl phosphate + O-D-mannosylprotein Pir2/hsp150
dolichyl phosphate D-mannose + ribonuclease 2
dolichyl phosphate + ribonuclease 2-D-mannose
dolichyl phosphate D-mannose + RSPSPSTQ
dolichyl phosphate + O-D-mannosyl-RSPSPSTQ
-
-
-
?
dolichyl phosphate D-mannose + Tyr-Ala-Thr-Ala-Val
dolichyl phosphate + O-D-mannosyl-Tyr-Ala-Thr-Ala-Val
dolichyl phosphate D-mannose + Tyr-Asn-Leu-Thr-Ser-Val
dolichyl phosphate + O-D-mannosyl-Tyr-Asn-Leu-Thr-Ser-Val
-
-
-
?
dolichyl phosphate D-mannose + Tyr-Asn-Pro-Thr-Ser-Val
dolichyl phosphate + O-D-mannosyl-Tyr-Asn-Pro-Thr-Ser-Val
dolichyl phosphate D-mannose + Tyr-Asn-Pro-Thr-Ser-Val-NH2
dolichyl phosphate + O-alpha-D-mannosyl-Tyr-Asn-Pro-Thr-Ser-Val-NH2
-
-
-
?
dolichyl phosphate D-mannose + Tyr-Leu-Thr-Ala-Val
dolichyl phosphate + O-D-mannosyl-Tyr-Leu-Thr-Ala-Val
-
-
-
?
dolichyl phosphate D-mannose + Tyr-Pro-Thr-Ala-Val
dolichyl phosphate + O-D-mannosyl-Tyr-Pro-Thr-Ala-Val
-
-
-
?
dolichyl beta-D-mannosyl phosphate + L-seryl-[protein]
dolichyl phosphate + 3-O-(alpha-D-mannosyl)-L-seryl-[protein]
-
-
-
?
dolichyl beta-D-mannosyl phosphate + L-seryl-[protein]
dolichyl phosphate + 3-O-(alpha-D-mannosyl)-L-seryl-[protein]
-
-
-
?
dolichyl beta-D-mannosyl phosphate + L-threonyl-[protein]
dolichyl phosphate + 3-O-(alpha-D-mannosyl)-L-threonyl-[protein]
-
-
-
?
dolichyl beta-D-mannosyl phosphate + L-threonyl-[protein]
dolichyl phosphate + 3-O-(alpha-D-mannosyl)-L-threonyl-[protein]
substrates used are Dol-P-[3H]mannose and 3.5 mM acceptor peptide Ac-YATAV-NH2
-
-
?
dolichyl beta-D-mannosyl phosphate + L-threonyl-[protein]
dolichyl phosphate + 3-O-(alpha-D-mannosyl)-L-threonyl-[protein]
-
-
-
?
dolichyl beta-D-mannosyl phosphate + L-threonyl-[protein]
dolichyl phosphate + 3-O-(alpha-D-mannosyl)-L-threonyl-[protein]
substrates used are Dol-P-[3H]mannose and 3.5 mM acceptor peptide Ac-YATAV-NH2
-
-
?
dolichyl phosphate D-mannose + Ac-Tyr-Ala-Thr-Ala-Val-NH2
dolichyl phosphate + O-D-mannosyl-Ac-Tyr-Ala-Thr-Ala-Val-NH2
-
-
-
?
dolichyl phosphate D-mannose + Ac-Tyr-Ala-Thr-Ala-Val-NH2
dolichyl phosphate + O-D-mannosyl-Ac-Tyr-Ala-Thr-Ala-Val-NH2
-
recombinant yeast overproducing PMT1 and PMT2
-
ir
dolichyl phosphate D-mannose + Ac-Tyr-Ala-Thr-Ala-Val-NH2
dolichyl phosphate + O-D-mannosyl-Ac-Tyr-Ala-Thr-Ala-Val-NH2
-
PMT1
-
?
dolichyl phosphate D-mannose + Ac-Tyr-Ala-Thr-Ala-Val-NH2
dolichyl phosphate + O-D-mannosyl-Ac-Tyr-Ala-Thr-Ala-Val-NH2
-
PMT1 transfers preferably to the threonine and valine residues, the additional enzyme form prefers the serine residue, both depending on the sequence of the acceptor substrate peptide
-
?
dolichyl phosphate D-mannose + Ac-Tyr-Asn-Pro-Thr-Ser-Val-NH2
dolichyl phosphate + O-D-mannosyl-Ac-Tyr-Asn-Pro-Thr-Ser-Val-NH2
-
-
-
?
dolichyl phosphate D-mannose + Ac-Tyr-Asn-Pro-Thr-Ser-Val-NH2
dolichyl phosphate + O-D-mannosyl-Ac-Tyr-Asn-Pro-Thr-Ser-Val-NH2
-
-
-
?
dolichyl phosphate D-mannose + Ac-Tyr-Asn-Pro-Thr-Ser-Val-NH2
dolichyl phosphate + O-D-mannosyl-Ac-Tyr-Asn-Pro-Thr-Ser-Val-NH2
-
-
?
dolichyl phosphate D-mannose + Ac-Tyr-Asn-Pro-Thr-Ser-Val-NH2
dolichyl phosphate + O-D-mannosyl-Ac-Tyr-Asn-Pro-Thr-Ser-Val-NH2
-
-
-
ir
dolichyl phosphate D-mannose + AcSSSSSNH2
dolichyl phosphate + O-D-mannosyl-AcSSSSSNH2
-
-
-
ir
dolichyl phosphate D-mannose + AcSSSSSNH2
dolichyl phosphate + O-D-mannosyl-AcSSSSSNH2
-
PMT1-3, PMT5, PMT6, not PMT4
-
?
dolichyl phosphate D-mannose + biotin-Tyr-Ala-Thr-Ala-Val-NH2
dolichyl phosphate + O-D-mannosyl-N-biotinyl-Tyr-Ala-Thr-Ala-Val-NH2
-
-
-
?
dolichyl phosphate D-mannose + biotin-Tyr-Ala-Thr-Ala-Val-NH2
dolichyl phosphate + O-D-mannosyl-N-biotinyl-Tyr-Ala-Thr-Ala-Val-NH2
-
-
-
?
dolichyl phosphate D-mannose + glucoamylase I
dolichyl phosphate + O-D-mannosyl glucoamylase I
-
-
-
?
dolichyl phosphate D-mannose + glucoamylase I
dolichyl phosphate + O-D-mannosyl glucoamylase I
the AaPmtA protein is involved in the formation of the normal cell wall. AaPmtA protein is responsible for the transfer of mannose to glucoamylase I
-
-
?
dolichyl phosphate D-mannose + glutathione-S-transferase fusion alpha-dystroglycan
dolichyl phosphate + O-D-mannosyl-glutathione-S-transferase fusion alpha-dystroglycan
-
-
-
-
?
dolichyl phosphate D-mannose + glutathione-S-transferase fusion alpha-dystroglycan
dolichyl phosphate + O-D-mannosyl-glutathione-S-transferase fusion alpha-dystroglycan
-
-
-
-
?
dolichyl phosphate D-mannose + human ribonuclease 2
dolichyl phosphate + human ribonuclease 2-D-mannose
-
whole protein or N-terminal dodecapeptide containing Trp7
D-mannose is bound at Trp7 forming a C-C linkage
?
dolichyl phosphate D-mannose + human ribonuclease 2
dolichyl phosphate + human ribonuclease 2-D-mannose
-
C-mannosylation activity
D-mannose is bound at Trp7 forming a C-C linkage
?
dolichyl phosphate D-mannose + human ribonuclease 2
dolichyl phosphate + human ribonuclease 2-D-mannose
-
no C-mannosylation activity of Trp7 when Trp10 is exchanged for Ala in the acceptor substrate
D-mannose is bound at Trp7 forming a C-C linkage
?
dolichyl phosphate D-mannose + human ribonuclease 2
dolichyl phosphate + human ribonuclease 2-D-mannose
-
recombinant wild-type RNase from E. coli is no substrate
D-mannose is bound at Trp7 forming a C-C linkage
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
the enzyme transfers mannosyl residues to the hydroxyl of serine or threonine residues
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
the enzyme transfers mannosyl residues to the hydroxyl of serine or threonine residues
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
production of cell-wall mannoproteins
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
the enzyme transfers mannosyl residues to the hydroxyl of serine or threonine residues
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
production of cell-wall mannoproteins
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
central role for Pmt4-mediated protein O-mannosylation in growth, cell wall integrity, and virulence of Cryptococcus neoformans
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
-
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
catalyzes the initial step of O-mannosyl glycan biosynthesis
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
synthetic peptides based on a mucin-like domain in alpha-dystroglycan. Thr414 of peptide 401-420 and Thr351 of peptide 336-355 are prominently modified by O-mannosylation
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
role of O-glycosylation in the control of folding of secretory proteins in the endoplasmic reticulum
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
-
-
ir
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
acceptor substrate: human-granulocyte-macrophage colony-stimulating-factor-derived peptide(4-11)
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
the enzyme transfers mannosyl residues to the hydroxyl of serine or threonine residues
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
the enzyme transfers mannosyl residues to the hydroxyl of serine or threonine residues
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
the enzyme transfers mannosyl residues to the hydroxyl of serine or threonine residues
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
the enzyme transfers mannosyl residues to the hydroxyl of serine or threonine residues
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
the enzyme transfers mannosyl residues to the hydroxyl of serine or threonine residues
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
the enzyme transfers mannosyl residues to the hydroxyl of serine or threonine residues
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
the enzyme transfers mannosyl residues to the hydroxyl of serine or threonine residues
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
the enzyme transfers mannosyl residues to the hydroxyl of serine or threonine residues
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
the enzyme transfers mannosyl residues to the hydroxyl of serine or threonine residues
-
ir
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
the enzyme transfers mannosyl residues to the hydroxyl of serine or threonine residues
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
preferred chain lengthin decreasing order: C100, C80, C55, C35
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
preferred chain lengthin decreasing order: C100, C80, C55, C35
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
acceptor substrate specificity study
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
strictly stereospecific for the anomeric configuration of phosphoryl-linkage of the donor substrate, a saturated alpha-isoprene unit in the dolichyl moiety is required
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
acidic amino acids strongly inhibit acceptor activity, as do glycine and proline residues as amino-terminal and carboxy-terminal neighbours
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
acceptor substrate: HCl-treated cell wall mannoprotein from Saccharomyces cerevisiae
-
ir
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
acceptor substrate specificities of PMT1-4,6
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
acceptor substrates: secretory proteins
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
acceptor substrates: secretory proteins
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
production of cell-wall mannoproteins
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
production of cell-wall mannoproteins
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
production of cell-wall mannoproteins
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-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
production of cell-wall mannoproteins
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-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
O-glycosylation initiated by Ogm proteins plays crucial physiological roles and can serve as a sorting determinant for protein transport of membrane glycoproteins. None of the ogm genes is found to be essential
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-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
O-glycosylation initiated by Ogm proteins plays crucial physiological roles and can serve as a sorting determinant for protein transport of membrane glycoproteins. None of the ogm genes is found to be essential. ogm4D mutants differ morphologically from wild type and exhibit defects in sexual agglutination
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-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
O-glycosylation initiated by Ogm proteins plays crucial physiological roles and can serve as a sorting determinant for protein transport of membrane glycoproteins. While none of the ogm genes is found to be essential, ogm1D mutants differ morphologically from wildtype and exhibit defects in sexual agglutination. O-glycosylation of chitinase from Saccharomyces cerevisiae is decreased in ogm1D cells
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-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
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protein O-mannosylation is crucial for cell wall integrity, septation and viability
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-
?
dolichyl phosphate D-mannose + protein Aga2
dolichyl phosphate + O-D-mannosylprotein Aga2
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i.e. small-agglutinin
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?
dolichyl phosphate D-mannose + protein Aga2
dolichyl phosphate + O-D-mannosylprotein Aga2
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activity is not affected by disruption mutations of PMT1-4
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?
dolichyl phosphate D-mannose + protein Aga2
dolichyl phosphate + O-D-mannosylprotein Aga2
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protein is located at the cell surface
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-
?
dolichyl phosphate D-mannose + protein AN5660
dolichyl phosphate + O-D-mannosylprotein
the un-glycosylated 32 kDa protein is an ortholog of Wsc family proteins in Saccharomyces cerevisiae, these proteins serve as sensors of stress, such as high temperature and cell wall-perturbing chemicals
AN5660
-
?
dolichyl phosphate D-mannose + protein AN5660
dolichyl phosphate + O-D-mannosylprotein
the non-glycosylated 32 kDa protein is an ortholog of Wsc family proteins in Saccharomyces cerevisiae, these proteins serve as sensors of stress, such as high temperature and cell wall-perturbing chemicals, S-tagged AN5660 is hypo-glycosylated in the deltapmtA and deltapmtC deletion mutants (target for these isoforms), not in the deltapmtB deletion mutant (no target)
AN5660
-
?
dolichyl phosphate D-mannose + protein AN5660
dolichyl phosphate + O-D-mannosylprotein
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triple-hemagglutin-tagged AN5660.3 protein is an ortholog of Wsc1 protein of Saccharomyces cerevisiae, a sensor for cell wall stress, underglycosylation upon AnpmtA and AnpmtC diruption not due to AnpmtB disruption
AN5660
-
?
dolichyl phosphate D-mannose + protein Bar1
dolichyl phosphate + O-D-mannosylprotein Bar1
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PMT1 and PMT2, not PMT3 and PMT4
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?
dolichyl phosphate D-mannose + protein Bar1
dolichyl phosphate + O-D-mannosylprotein Bar1
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protein is located in the medium
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-
?
dolichyl phosphate D-mannose + protein chitinase 1
dolichyl phosphate + O-D-mannosylprotein chitinase 1
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PMT1
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?
dolichyl phosphate D-mannose + protein chitinase 1
dolichyl phosphate + O-D-mannosylprotein chitinase 1
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PMT1, PMT4, PMT6 and especially PMT2, not PMT3
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?
dolichyl phosphate D-mannose + protein chitinase 1
dolichyl phosphate + O-D-mannosylprotein chitinase 1
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protein is located in the cell wall and medium
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-
?
dolichyl phosphate D-mannose + protein Ggp1/Gas1
dolichyl phosphate + O-D-mannosylprotein Ggp1/Gas1
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PMT4 and PMT6, not PMT1-3
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?
dolichyl phosphate D-mannose + protein Ggp1/Gas1
dolichyl phosphate + O-D-mannosylprotein Ggp1/Gas1
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protein is located at the cell surface
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-
?
dolichyl phosphate D-mannose + protein Kex2
dolichyl phosphate + O-D-mannosylprotein Kex2
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PMT4, not PMT1-3
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?
dolichyl phosphate D-mannose + protein Kex2
dolichyl phosphate + O-D-mannosylprotein Kex2
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protein is located in the Golgi apparatus
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-
?
dolichyl phosphate D-mannose + protein Kre9
dolichyl phosphate + O-D-mannosylprotein Kre9
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mainly PMT1 and PMT2, not PMT3 and PMT4
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?
dolichyl phosphate D-mannose + protein Kre9
dolichyl phosphate + O-D-mannosylprotein Kre9
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protein is located in the Golgi apparatus
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-
?
dolichyl phosphate D-mannose + protein Pir2/hsp150
dolichyl phosphate + O-D-mannosylprotein Pir2/hsp150
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PMT1
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?
dolichyl phosphate D-mannose + protein Pir2/hsp150
dolichyl phosphate + O-D-mannosylprotein Pir2/hsp150
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PMT1, PMT2, and to some extent PMT4, not PMT3
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?
dolichyl phosphate D-mannose + protein Pir2/hsp150
dolichyl phosphate + O-D-mannosylprotein Pir2/hsp150
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protein is located in the medium
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-
?
dolichyl phosphate D-mannose + ribonuclease 2
dolichyl phosphate + ribonuclease 2-D-mannose
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C-mannosylation activity
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-
?
dolichyl phosphate D-mannose + ribonuclease 2
dolichyl phosphate + ribonuclease 2-D-mannose
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C-mannosylation activity
D-mannose is bound at Trp7 forming a C-C linkage
?
dolichyl phosphate D-mannose + ribonuclease 2
dolichyl phosphate + ribonuclease 2-D-mannose
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biosynthetic pathway
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-
?
dolichyl phosphate D-mannose + Tyr-Ala-Thr-Ala-Val
dolichyl phosphate + O-D-mannosyl-Tyr-Ala-Thr-Ala-Val
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-
-
?
dolichyl phosphate D-mannose + Tyr-Ala-Thr-Ala-Val
dolichyl phosphate + O-D-mannosyl-Tyr-Ala-Thr-Ala-Val
wild-type and mutants
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?
dolichyl phosphate D-mannose + Tyr-Asn-Pro-Thr-Ser-Val
dolichyl phosphate + O-D-mannosyl-Tyr-Asn-Pro-Thr-Ser-Val
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-
-
?
dolichyl phosphate D-mannose + Tyr-Asn-Pro-Thr-Ser-Val
dolichyl phosphate + O-D-mannosyl-Tyr-Asn-Pro-Thr-Ser-Val
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-
-
?
dolichyl phosphate D-mannose + Tyr-Asn-Pro-Thr-Ser-Val
dolichyl phosphate + O-D-mannosyl-Tyr-Asn-Pro-Thr-Ser-Val
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-
-
?
dolichyl phosphate D-mannose + Tyr-Asn-Pro-Thr-Ser-Val
dolichyl phosphate + O-D-mannosyl-Tyr-Asn-Pro-Thr-Ser-Val
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-
-
?
dolichyl phosphate D-mannose + Tyr-Asn-Pro-Thr-Ser-Val
dolichyl phosphate + O-D-mannosyl-Tyr-Asn-Pro-Thr-Ser-Val
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-
-
?
additional information
?
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-
Afpmt1 acts as an O-mannosyltransferase. Characterization of the DELTAAfpmt1 mutant shows that a lack of AfPmt1p results in sensitivity to elevated temperature and defects in growth and cell wall integrity, thereby affecting cell morphology, conidium formation, and germination. In a mouse model, Afpmt1 is not required for the virulence of Aspergillus fumigatus
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?
additional information
?
-
-
PMT4 is required for full virulence of Candida albicans
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-
?
additional information
?
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-
PMT5 does not make a significant contribution to virulence
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-
?
additional information
?
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-
protein mannosyltransferases (Pmt proteins Pmt1p, Pmt2p, Pmt4p, Pmt5p, and Pmt6p) initiate O mannosylation of secretory proteins. Virulence of the fungal pathogen Candida albicans requires the five isoforms of protein mannosyltransferases. The importance of individual Pmt isoforms may differ in specific host niches
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?
additional information
?
-
protein mannosyltransferases (Pmt proteins Pmt1p, Pmt2p, Pmt4p, Pmt5p, and Pmt6p) initiate O mannosylation of secretory proteins. Virulence of the fungal pathogen Candida albicans requires the five isoforms of protein mannosyltransferases. The importance of individual Pmt isoforms may differ in specific host niches
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-
?
additional information
?
-
protein mannosyltransferases (Pmt proteins Pmt1p, Pmt2p, Pmt4p, Pmt5p, and Pmt6p) initiate O mannosylation of secretory proteins. Virulence of the fungal pathogen Candida albicans requires the five isoforms of protein mannosyltransferases. The importance of individual Pmt isoforms may differ in specific host niches
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-
?
additional information
?
-
protein mannosyltransferases (Pmt proteins Pmt1p, Pmt2p, Pmt4p, Pmt5p, and Pmt6p) initiate O mannosylation of secretory proteins. Virulence of the fungal pathogen Candida albicans requires the five isoforms of protein mannosyltransferases. The importance of individual Pmt isoforms may differ in specific host niches
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-
?
additional information
?
-
protein mannosyltransferases (Pmt proteins Pmt1p, Pmt2p, Pmt4p, Pmt5p, and Pmt6p) initiate O mannosylation of secretory proteins. Virulence of the fungal pathogen Candida albicans requires the five isoforms of protein mannosyltransferases. The importance of individual Pmt isoforms may differ in specific host niches
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-
?
additional information
?
-
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protein O-mannosyltransferase isoforms regulate biofilm formation in Candida albicans
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-
?
additional information
?
-
O-mannosylation of specific secretory proteins of the human fungal pathogen Candida albicans contributes significantly to virulence
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-
?
additional information
?
-
O-mannosylation of specific secretory proteins of the human fungal pathogen Candida albicans contributes significantly to virulence
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-
?
additional information
?
-
O-mannosylation of specific secretory proteins of the human fungal pathogen Candida albicans contributes significantly to virulence
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-
?
additional information
?
-
O-mannosylation of specific secretory proteins of the human fungal pathogen Candida albicans contributes significantly to virulence
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-
?
additional information
?
-
O-mannosylation of specific secretory proteins of the human fungal pathogen Candida albicans contributes significantly to virulence
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-
?
additional information
?
-
O-mannosylation of specific secretory proteins of the human fungal pathogen Candida albicans contributes significantly to virulence. PMT2 is essential for growth. Loss of a single PMT2 allele already sufficed to significantly retarded growth
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-
?
additional information
?
-
O-mannosylation of specific secretory proteins of the human fungal pathogen Candida albicans contributes significantly to virulence. PMT2 is essential for growth. Loss of a single PMT2 allele already sufficed to significantly retarded growth
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-
?
additional information
?
-
O-mannosylation of specific secretory proteins of the human fungal pathogen Candida albicans contributes significantly to virulence. PMT2 is essential for growth. Loss of a single PMT2 allele already sufficed to significantly retarded growth
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-
?
additional information
?
-
O-mannosylation of specific secretory proteins of the human fungal pathogen Candida albicans contributes significantly to virulence. PMT2 is essential for growth. Loss of a single PMT2 allele already sufficed to significantly retarded growth
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-
?
additional information
?
-
O-mannosylation of specific secretory proteins of the human fungal pathogen Candida albicans contributes significantly to virulence. PMT2 is essential for growth. Loss of a single PMT2 allele already sufficed to significantly retarded growth
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-
?
additional information
?
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Drosophila sp. (in: flies)
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protein O-mannosyltransferases 1 and 2 are required to maintain integrity of Drosophila larval muscles
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-
?
additional information
?
-
-
O-mannosylation of specific secretory proteins of the bacterial pathogen Mycobacterium tuberculosis contributes significantly to virulence
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-
?
additional information
?
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-
although the improved secretion of the protein by suppression of O mannosylation might not be a general phenomenon, the suppression of O mannosylation could be beneficial for the production of proteins forming either homomeric or heteromeric complexes through their hydrophobic interaction in yeast
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-
?
additional information
?
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-
PMT3: no clearly determined dolichyl-phosphate-mannose-protein mannosyltransferase activity
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-
?
additional information
?
-
-
PMT4 and PMT6 probably function as an active dimer
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-
?
additional information
?
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-
PMT1 and PMT2 function as a complex
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-
?
additional information
?
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-
PMT1 and PMT2 function as a complex
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-
?
additional information
?
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-
PMT3 behaves as a dolichyl-phosphate-mannose-glycolipid alpha-mannosyltransferase, EC 2.4.1.130
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-
?
additional information
?
-
PMT3 behaves as a dolichyl-phosphate-mannose-glycolipid alpha-mannosyltransferase, EC 2.4.1.130
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-
?
additional information
?
-
PMT3 behaves as a dolichyl-phosphate-mannose-glycolipid alpha-mannosyltransferase, EC 2.4.1.130
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-
?
additional information
?
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-
defective mutants are used to investigate the substrate specificities of PMT1-4,6 in vivo
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-
?
additional information
?
-
disruption of the pmt1 gene decreased protein secretion but has no effect on glycosylation of secreted proteins. PMTI protein O-mannosyltranferase does not take part in glycosylation of these proteins
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-
?
additional information
?
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-
disruption of the pmt1 gene decreased protein secretion but has no effect on glycosylation of secreted proteins. PMTI protein O-mannosyltranferase does not take part in glycosylation of these proteins
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?
