Information on EC 2.4.1.109 - dolichyl-phosphate-mannose-protein mannosyltransferase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY
2.4.1.109
-
RECOMMENDED NAME
GeneOntology No.
dolichyl-phosphate-mannose-protein mannosyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
dolichyl phosphate D-mannose + protein = dolichyl phosphate + O-D-mannosylprotein
show the reaction diagram
structure-function analysis
-
dolichyl phosphate D-mannose + protein = dolichyl phosphate + O-D-mannosylprotein
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
hexosyl group transfer
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Other types of O-glycan biosynthesis
-
SYSTEMATIC NAME
IUBMB Comments
dolichyl-phosphate-D-mannose:protein O-D-mannosyltransferase
The enzyme transfers mannosyl residues to the hydroxy group of serine or threonine residues, producing cell-wall mannoproteins. It acts only on long-chain alpha-dihydropolyprenyl derivatives, larger than C35.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
AapmtA
Q96VV1
-
AnPmtA
-
PMT2 subfamily
AnPmtB
-
PMT1 subfamily
AnPmtC
-
PMT4 subfamily
dolichol phosphomannose-protein mannosyltransferase
-
-
-
-
dolichyl-phosphate-mannose--protein mannosyltransferase 1
O13898
-
dolichyl-phosphate-mannose--protein mannosyltransferase 2
Q9C100
-
dolichyl-phosphate-mannose--protein mannosyltransferase 4
O42933
-
dolichyl-phosphate-mannose-protein mannosyltransferase
-
-
dolichyl-phosphate-mannose-protein mannosyltransferase 1
-
-
dolichyl-phosphate-mannose-protein mannosyltransferase 1
-
-
dolichyl-phosphate-mannose-protein mannosyltransferase 1
Q99PR0
-
dolichyl-phosphate-mannose-protein mannosyltransferase 2
Q14U74
-
Drosophila O-mannosyltransferase Rotated Abdomen
-
-
Drosophila O-mannosyltransferase Twisted
-
-
HpPmt1p
Q66VU5
-
O-glycoside mannosyltransferase
O13898, O42933, Q9C100
-
O-mannosyltransferase
-
-
O-mannosyltransferase
-
-
O-mannosyltransferase
Q9Y6A1
-
O-mannosyltransferase
-
-
O-mannosyltransferase
Q4P140, Q4P339, Q4P380
-
O-mannosyltransferase 1
-
-
PMT
P33775, P42934
-
PMT
P52867, Q06644
-
PMT1
Q4P140
-
Pmt1p-Pmt2p
-
-
PMT2
Q4P339
-
PMT4
Q4P380
-
Pmt4p
-
-
PMT5
Q5ACU3
-
PmtA
Q96WN5
Pmt-2 subfamily
pmtB
Q5B3W9
Pmt-1 subfamily
pmtC
Q5BDC1
Pmt-4 subfamily
POMT1
-
; isoform
POMT1
-
-
POMT1
Q99PR0
-
POMT2
-
; isoform
POMT2
Q9UKY4
-
POMT2
Q14U74
-
protein mannosyltransferase
-
-
protein mannosyltransferases
-
-
protein O-D-mannosyltransferase
-
-
-
-
protein O-mannosyl-transferase 1
Q9Y6A1
-
protein O-mannosyl-transferase 1
Q99PR0
-
protein O-mannosyl-transferase 2
Q9UKY4
-
protein O-mannosyl-transferase 2
Q14U74
-
protein O-mannosyltransferase
-
-
protein O-mannosyltransferase
Q5KAF1, Q5KHK5, Q5KIZ1
-
protein O-mannosyltransferase
Q5B3W9, Q5BDC1, Q96WN5
-
protein O-mannosyltransferase
-
-
protein O-mannosyltransferase
-
-
protein O-mannosyltransferase
-
-
protein O-mannosyltransferase 1
-
-
protein O-mannosyltransferase 1
-
-
protein O-mannosyltransferase 1
Q9Y6A1
-
protein O-mannosyltransferase 2
-
-
protein O-mannosyltransferase 2
-
-
protein O-mannosyltransferase 2
Q9UKY4
-
protein O-mannosyltransferase A
Q96VV1
-
protein O-mannosyltransferase Pmt4
A3E242
-
protein O-mannosyltransferases 1
-
-
protein O-mannosyltransferases 2
-
-
protein-O-mannosyltransferase-1
Q9Y6A1
-
sPOMT2
-
-
tPOmt2
-
-
Um05433
Q4P380
-
Um10749
Q4P339
-
Um11220
Q4P140
-
mannosyltransferase, dolichol phosphomannose-protein
-
-
-
-
additional information
-
-
additional information
-
PMT3: no clearly determined dolichyl-phosphate-mannose-protein mannosyltransferase activity
additional information
P46971, P47190
PMT3 behaves as a dolichyl-phosphate-mannose-glycolipid alpha-mannosyltransferase, EC 2.4.1.130
CAS REGISTRY NUMBER
COMMENTARY
74315-99-4
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
putative
SwissProt
Manually annotated by BRENDA team
strain ATCC 26555
-
-
Manually annotated by BRENDA team
Candida albicans 2005 E
2005 E
-
-
Manually annotated by BRENDA team
serotype A, wild-type strain H99, human fungal pathogen, strain used for pathogenesis experiments
-
-
Manually annotated by BRENDA team
serotype D, wild-type strain JEC21 and JEC21, human fungal pathogen, strain used for pathogenesis experiments
UniProt
Manually annotated by BRENDA team
wild-type strain A850 (gene templates and control), and deletion mutants
UniProt
Manually annotated by BRENDA team
one patient with limb girdle muscular dystrophy 2K, one patient with Walker-Warburg syndrome
SwissProt
Manually annotated by BRENDA team
C-mannosylating enzyme
-
-
Manually annotated by BRENDA team
enzyme form other than PMT1; gene PMT1
-
-
Manually annotated by BRENDA team
enzyme form other than PMT2; gene PMT1
-
-
Manually annotated by BRENDA team
gene PMT1
SwissProt
Manually annotated by BRENDA team
gene PMT1; gene PMT2
-
-
Manually annotated by BRENDA team
gene PMT5
SwissProt
Manually annotated by BRENDA team
gene PMT6
SwissProt
Manually annotated by BRENDA team
gene PMT7
SwissProt
Manually annotated by BRENDA team
genes PMT1-6
-
-
Manually annotated by BRENDA team
strain BY4743
-
-
Manually annotated by BRENDA team
fungal plant pathogen
-
-
Manually annotated by BRENDA team
maize smut fungus causes tumor formation in Zea mays, strains FB1, FB2 strains, AB33, and AB34
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
malfunction
-
AnpmtA + AnpmtB double disruptant is viable but slow growing with morphological characteristics cumulative of single disruptants; AnpmtA + AnpmtB double disruptant is viable but slow growing with morphological characteristics cumulative of single disruptants, hyperglycosylation of specific target proteins; AnpmtB disruptant shows wild-type colony formation at 30C, slightly repressed growth at 42C, conidiation reduced to about 50%, hyperbranching of hyphae (defect in polarity maintenance); pmtC disruptant with highest growth repression, swollen, frequently branched hyphae, no conidia formation, recovery of hyphal structures in the presence of osmotic stabilizers, enables conidiophore and conidia production (abnormal and fewer) at 42C
malfunction
Q5B3W9, Q5BDC1, Q96WN5
single enzyme deletion mutants are viable, at elevated temperatures they show cell wall-associated defects and increased sensitivity to cell wall-perturbing agents, and defects in developmental patterning, partial restoration of wild-type growth with the osmotic sorbitol; single enzyme deletion mutants are viable, at elevated temperatures they show cell wall-associated defects and increased sensitivity to cell wall-perturbing agents, and defects in developmental patterning, partial restoration of wild-type growth with the osmotic sorbitol; single enzyme deletion mutants are viable, at elevated temperatures they show cell wall-associated defects and increased sensitivity to cell wall-perturbing agents, and defects in developmental patterning, partial restoration of wild-type growth with the osmotic sorbitol
malfunction
-
defects in O-mannosylation are associated with muscular dystrophies (dystroglycanopathies)
malfunction
-
mutation in either one of the complex forming enzymes can lead to Walker-Warburg syndrome, a congenital muscular dystrophy with abnormal neuronal migration
malfunction
Q9Y6A1
dystroglycanopathies (muscular dystrophy due to abnormal glycosylation of alpha-dystroglycan) such as the severe Walker-Warburg syndrome (brain and eye abnormalities, mild limb girdle muscular dystrophy)
malfunction
Q4P140, Q4P339, Q4P380
pmt4 deletion mutant with strong reduction in appressorium formation, the few formed appressoria lack the capacity to penetrate the plant cuticle, reduced pathogenicity, no effects on vegetative growth or mating, normal polar growth of infectious hyphae
malfunction
-
loss of the O-mannosyltransferase is associated with a reduced formation frequency of the invasive structure, the appressorium, combined with a loss in the ability to penetrate the plant cuticle
malfunction
-
virulence of the human fungal pathogen causing meningoencephalitis depends on extracellular factors including the O-glycosylation of proteins
malfunction
Q5KAF1, Q5KHK5, Q5KIZ1
virulence of the human fungal pathogen causing meningoencephalitis depends on extracellular factors including the O-glycosylation of proteins; virulence of the human fungal pathogen causing meningoencephalitis depends on extracellular factors including the O-glycosylation of proteins; virulence of the human fungal pathogen causing meningoencephalitis depends on extracellular factors including the O-glycosylation of proteins
metabolism
-
a complex of protein O-mannosyltransferase 1 and 2 catalyzes the initial step of O-mannosyl glycan biosynthesis; isoforms POMT1 and POMT2 catalyze the initial step of O-mannosyl glycan biosynthesis
metabolism
-
protein O-mannosyltransferase 1 (POMT1) and its homolog, POMT2, are responsible for the catalysis of the first step in O-mannosyl glycan synthesis
physiological function
-
AnpmtB, hyphal development and differentiation, polarity maintenance; AnpmtC, hyphal development and differentiation, maintenance of cell wall integrity; fungal morphology and conidia formation
physiological function
Q5B3W9, Q5BDC1, Q96WN5
role in cell wall integrity pathway and developmental patterning by providing spatial cues; role in cell wall integrity pathway and developmental patterning by providing spatial cues; role in cell wall integrity pathway and developmental patterning by providing spatial cues
physiological function
-
O-mannosylation can modulate the ligand-binding activity of alpha-dystroglycan
physiological function
Q4P140, Q4P339, Q4P380
pmt4 is important for pathogenesis (appressorium formation and penetration)
physiological function
-
O-mannosylation is essential for virulence of the fungus
physiological function
-
O-glycosylation of proteins
physiological function
Q5KAF1, Q5KHK5, Q5KIZ1
O-glycosylation of proteins; O-glycosylation of proteins; O-glycosylation of proteins
physiological function
-
the Pmt1p-Pmt2p complex participates in endoplasmic reticulum protein quality control. The Pmt1p-Pmt2p complex is required for the fast endoplasmic reticulum exit of wild-type substrate Gas1p
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
dolichyl phosphate D-mannose + Ac-Ala-Thr-Ala-NH2
dolichyl phosphate + O-D-mannosyl-Ac-Ala-Thr-Ala-NH2
show the reaction diagram
-
-
-
?
dolichyl phosphate D-mannose + Ac-Tyr-Ala-Thr-Ala-Val-NH2
dolichyl phosphate + O-D-mannosyl-Ac-Tyr-Ala-Thr-Ala-Val-NH2
show the reaction diagram
-
-
-
?
dolichyl phosphate D-mannose + Ac-Tyr-Ala-Thr-Ala-Val-NH2
dolichyl phosphate + O-D-mannosyl-Ac-Tyr-Ala-Thr-Ala-Val-NH2
show the reaction diagram
-
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
show the reaction diagram
-
PMT1
-
?
dolichyl phosphate D-mannose + Ac-Tyr-Ala-Thr-Ala-Val-NH2
dolichyl phosphate + O-D-mannosyl-Ac-Tyr-Ala-Thr-Ala-Val-NH2
show the reaction diagram
-
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
show the reaction diagram
P31382, -
-
-
?
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
show the reaction diagram
-
-
-
ir
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
show the reaction diagram
Candida albicans, Candida albicans 2005 E
-
-
-
?
dolichyl phosphate D-mannose + AcSSSSSNH2
dolichyl phosphate + O-D-mannosyl-AcSSSSSNH2
show the reaction diagram
-
-
-
ir
dolichyl phosphate D-mannose + AcSSSSSNH2
dolichyl phosphate + O-D-mannosyl-AcSSSSSNH2
show the reaction diagram
-
PMT1-3, PMT5, PMT6, not PMT4
-
?
dolichyl phosphate D-mannose + alpha-dystroglycan
dolichyl phosphate + O-D-mannosyl-[alpha-dystroglycan]
show the reaction diagram
-
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]
show the reaction diagram
Q9Y6A1
sugar donor tritium-labeled
-
-
?
dolichyl phosphate D-mannose + Asn-Ala-Thr-Val-dinitrophenyl
dolichyl phosphate + O-D-mannosyl-Asn-Ala-Thr-Val-dinitrophenyl
show the reaction diagram
-
-
-
?
dolichyl phosphate D-mannose + biotin-Tyr-Ala-Thr-Ala-Val-NH2
dolichyl phosphate + O-D-mannosyl-N-biotinyl-Tyr-Ala-Thr-Ala-Val-NH2
show the reaction diagram
-
-
-
?
dolichyl phosphate D-mannose + biotin-Tyr-Ala-Thr-Ala-Val-NH2
dolichyl phosphate + O-D-mannosyl-N-biotinyl-Tyr-Ala-Thr-Ala-Val-NH2
show the reaction diagram
-
-
-
?
dolichyl phosphate D-mannose + biotin-Tyr-Pro-Thr-Ala-Val-NH2
dolichyl phosphate + O-D-mannosyl-N-biotinyl-Tyr-Pro-Thr-Ala-Val-NH2
show the reaction diagram
-
-
-
?
dolichyl phosphate D-mannose + biotin-Tyr-Thr-Ala-Val-NH2
dolichyl phosphate + O-D-mannosyl-N-biotinyl-Tyr-Thr-Ala-Val-NH2
show the reaction diagram
-
-
-
?
dolichyl phosphate D-mannose + Gas1p
dolichyl phosphate + O-D-mannosyl-Gas1p
show the reaction diagram
-
-
-
-
?
dolichyl phosphate D-mannose + glucoamylase I
dolichyl phosphate + O-D-mannosyl glucoamylase I
show the reaction diagram
-, Q96VV1
-
-
-
?
dolichyl phosphate D-mannose + glucoamylase I
dolichyl phosphate + O-D-mannosyl glucoamylase I
show the reaction diagram
-, Q96VV1
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 + glucoamylase I
dolichyl phosphate + O-D-mannosyl-[glucoamylase]
show the reaction diagram
-
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-[alpha-dystroglycan]
show the reaction diagram
-
tritium-labeled sugar donor, 20 mM Tris-HCl, pH 8.0, 2-mercaptoethanol, EDTA, n-octyl-beta-D-thiogucoside, 22C
-
-
?
dolichyl phosphate D-mannose + glutathione-S-transferase fusion alpha-dystroglycan
dolichyl phosphate + O-D-mannosyl-glutathione-S-transferase fusion alpha-dystroglycan
show the reaction diagram
-
-
-
-
?
dolichyl phosphate D-mannose + glutathione-S-transferase fusion alpha-dystroglycan
dolichyl phosphate + O-D-mannosyl-glutathione-S-transferase fusion alpha-dystroglycan
show the reaction diagram
-
-
-
-
?
dolichyl phosphate D-mannose + glutathione-S-transferase fusion alpha-dystroglycan
dolichyl phosphate + O-D-mannosyl-[glutathione-S-transferase fusion alpha-dystroglycan]
show the reaction diagram
-
-
-
-
?
dolichyl phosphate D-mannose + human ribonuclease 2
dolichyl phosphate + human ribonuclease 2-D-mannose
show the reaction diagram
-
whole protein or N-terminal dodecapeptide containing Trp7, C-mannosylation activity, no C-mannosylation activity of Trp7 when Trp10 is exchanged for Ala in the acceptor substrate, 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 + Lys-Pro-Ser-Gly-Tyr
dolichyl phosphate + O-D-mannosyl-Lys-Pro-Ser-Gly-Tyr
show the reaction diagram
-
-
-
?
dolichyl phosphate D-mannose + Lys-Pro-Thr-Gly-Tyr
dolichyl phosphate + O-D-mannosyl-Lys-Pro-Thr-Gly-Tyr
show the reaction diagram
-
-
-
?
dolichyl phosphate D-mannose + Lys-Pro-Thr-Pro-Tyr
dolichyl phosphate + O-D-mannosyl-Lys-Pro-Thr-Pro-Tyr
show the reaction diagram
-
-
-
?
dolichyl phosphate D-mannose + N-acetyl-SSSSS
dolichyl phosphate + O-D-mannosyl-N-acetyl-SSSSS
show the reaction diagram
-
worst substrate
-
-
?
dolichyl phosphate D-mannose + N-acetyl-YASAV
dolichyl phosphate + O-D-mannosyl-N-acetyl-YASAV
show the reaction diagram
-
-
-
-
?
dolichyl phosphate D-mannose + N-acetyl-YATAV
dolichyl phosphate + O-D-mannosyl-N-acetyl-YATAV
show the reaction diagram
-
best substrate
-
-
?
dolichyl phosphate D-mannose + N-acetyl-YATAVK-biotin
dolichyl phosphate + O-D-mannosyl-N-acetyl-YATAVK-biotin
show the reaction diagram
-
N-acetyl-YATAVK-biotin preferentially reacts with isoform Pmt1p
-
-
?
dolichyl phosphate D-mannose + Pro-Thr-Val
dolichyl phosphate + O-D-mannosyl-Pro-Thr-Val
show the reaction diagram
-
-
-
?
dolichyl phosphate D-mannose + Pro-Tyr-Thr-Val
dolichyl phosphate + O-D-mannosyl-Pro-Tyr-Thr-Val
show the reaction diagram
-
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
show the reaction diagram
-
-
-
-
-
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
show the reaction diagram
P31382, -
-
-
-
-
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
show the reaction diagram
-
-
-
-
-
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
show the reaction diagram
-
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
show the reaction diagram
-
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
show the reaction diagram
P46971, P47190, -
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
show the reaction diagram
-
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
show the reaction diagram
-
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
show the reaction diagram
-
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
show the reaction diagram
-
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
show the reaction diagram
-
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
show the reaction diagram
P31382, -
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
show the reaction diagram
-
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
show the reaction diagram
-
-
-
ir
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
show the reaction diagram
-
-
-
-
-
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
show the reaction diagram
-
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
show the reaction diagram
-
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
show the reaction diagram
Q5KAF1, Q5KHK5, Q5KIZ1
-
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
show the reaction diagram
-
-
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
show the reaction diagram
-
acceptor substrate: human-granulocyte-macrophage colony-stimulating-factor-derived peptide(4-11)
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
show the reaction diagram
-
the enzyme transfers mannosyl residues to the hydroxyl of serine or threonine residues
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
show the reaction diagram
P46971, P47190, -
the enzyme transfers mannosyl residues to the hydroxyl of serine or threonine residues
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
show the reaction diagram
-
the enzyme transfers mannosyl residues to the hydroxyl of serine or threonine residues
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
show the reaction diagram
-
the enzyme transfers mannosyl residues to the hydroxyl of serine or threonine residues
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
show the reaction diagram
-
the enzyme transfers mannosyl residues to the hydroxyl of serine or threonine residues
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
show the reaction diagram
-
the enzyme transfers mannosyl residues to the hydroxyl of serine or threonine residues
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
show the reaction diagram
P31382, -
the enzyme transfers mannosyl residues to the hydroxyl of serine or threonine residues
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
show the reaction diagram
-
the enzyme transfers mannosyl residues to the hydroxyl of serine or threonine residues
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
show the reaction diagram
-
the enzyme transfers mannosyl residues to the hydroxyl of serine or threonine residues
-
ir
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
show the reaction diagram
-
the enzyme transfers mannosyl residues to the hydroxyl of serine or threonine residues
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
show the reaction diagram
-
the enzyme transfers mannosyl residues to the hydroxyl of serine or threonine residues
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
show the reaction diagram
P33775, P42934, P52867, Q06644
the enzyme transfers mannosyl residues to the hydroxyl of serine or threonine residues
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
show the reaction diagram
-
preferred chain lengthin decreasing order: C100, C80, C55, C35
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
show the reaction diagram
-
preferred chain lengthin decreasing order: C100, C80, C55, C35
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
show the reaction diagram
-
acceptor substrate specificity study
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
acceptor substrate: HCl-treated cell wall mannoprotein from Saccharomyces cerevisiae
-
ir
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
show the reaction diagram
-
acceptor substrate specificities of PMT1-4,6
-
-
-
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
show the reaction diagram
-
acceptor substrate specificities of PMT1-4,6
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
show the reaction diagram
P33775, P42934, P52867, Q06644
acceptor substrates: secretory proteins
-
-
-
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
show the reaction diagram
P33775, P42934, P52867, Q06644
acceptor substrates: secretory proteins
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
show the reaction diagram
-
production of cell-wall mannoproteins
-
-
-
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
show the reaction diagram
P46971, P47190, -
production of cell-wall mannoproteins
-
-
-
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
show the reaction diagram
-
production of cell-wall mannoproteins
-
-
-
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
show the reaction diagram
-
production of cell-wall mannoproteins
-
-
-
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
show the reaction diagram
P33775, P42934, P52867, Q06644
production of cell-wall mannoproteins
-
-
-
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
show the reaction diagram
-
catalyzes the initial step of O-mannosyl glycan biosynthesis
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
show the reaction diagram
A3E242, -
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
show the reaction diagram
O13898, O42933, Q9C100, -
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
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
show the reaction diagram
O13898, O42933, Q9C100, -
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
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
show the reaction diagram
O13898, O42933, Q9C100, -
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
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
show the reaction diagram
-
protein O-mannosylation is crucial for cell wall integrity, septation and viability
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
show the reaction diagram
-, Q66VU5
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
show the reaction diagram
-
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
show the reaction diagram
Candida albicans 2005 E
-
-, the enzyme transfers mannosyl residues to the hydroxyl of serine or threonine residues
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
show the reaction diagram
Candida albicans 2005 E
-
production of cell-wall mannoproteins
-
-
-
dolichyl phosphate D-mannose + protein Aga2
dolichyl phosphate + O-D-mannosylprotein Aga2
show the reaction diagram
-
i.e. small-agglutinin
-
-
-
dolichyl phosphate D-mannose + protein Aga2
dolichyl phosphate + O-D-mannosylprotein Aga2
show the reaction diagram
-
i.e. small-agglutinin
-
?
dolichyl phosphate D-mannose + protein Aga2
dolichyl phosphate + O-D-mannosylprotein Aga2
show the reaction diagram
-
activity is not affected by disruption mutations of PMT1-4
-
-
-
dolichyl phosphate D-mannose + protein Aga2
dolichyl phosphate + O-D-mannosylprotein Aga2
show the reaction diagram
-
activity is not affected by disruption mutations of PMT1-4
-
?
dolichyl phosphate D-mannose + protein Aga2
dolichyl phosphate + O-D-mannosylprotein Aga2
show the reaction diagram
-
protein is located at the cell surface
-
-
-
dolichyl phosphate D-mannose + protein AN5660
dolichyl phosphate + O-D-mannosylprotein
show the reaction diagram
Q5B3W9, Q5BDC1, Q96WN5
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
show the reaction diagram
Q5B3W9, Q5BDC1, Q96WN5
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
show the reaction diagram
-
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
show the reaction diagram
-
PMT1 and PMT2, not PMT3 and PMT4
-
-
-
dolichyl phosphate D-mannose + protein Bar1
dolichyl phosphate + O-D-mannosylprotein Bar1
show the reaction diagram
-
PMT1 and PMT2, not PMT3 and PMT4
-
?
dolichyl phosphate D-mannose + protein Bar1
dolichyl phosphate + O-D-mannosylprotein Bar1
show the reaction diagram
-
protein is located in the medium
-
-
-
dolichyl phosphate D-mannose + protein chitinase 1
dolichyl phosphate + O-D-mannosylprotein chitinase 1
show the reaction diagram
-
PMT1
-
-
-
dolichyl phosphate D-mannose + protein chitinase 1
dolichyl phosphate + O-D-mannosylprotein chitinase 1
show the reaction diagram
-
PMT1
-
?
dolichyl phosphate D-mannose + protein chitinase 1
dolichyl phosphate + O-D-mannosylprotein chitinase 1
show the reaction diagram
-
PMT1, PMT4, PMT6 and especially PMT2, not PMT3
-
-
-
dolichyl phosphate D-mannose + protein chitinase 1
dolichyl phosphate + O-D-mannosylprotein chitinase 1
show the reaction diagram
-
PMT1, PMT4, PMT6 and especially PMT2, not PMT3
-
?
dolichyl phosphate D-mannose + protein chitinase 1
dolichyl phosphate + O-D-mannosylprotein chitinase 1
show the reaction diagram
-
protein is located in the cell wall and medium
-
-
-
dolichyl phosphate D-mannose + protein Ggp1/Gas1
dolichyl phosphate + O-D-mannosylprotein Ggp1/Gas1
show the reaction diagram
-
PMT4 and PMT6, not PMT1-3
-
-
-
dolichyl phosphate D-mannose + protein Ggp1/Gas1
dolichyl phosphate + O-D-mannosylprotein Ggp1/Gas1
show the reaction diagram
-
PMT4 and PMT6, not PMT1-3
-
?
dolichyl phosphate D-mannose + protein Ggp1/Gas1
dolichyl phosphate + O-D-mannosylprotein Ggp1/Gas1
show the reaction diagram
-
protein is located at the cell surface
-
-
-
dolichyl phosphate D-mannose + protein Kex2
dolichyl phosphate + O-D-mannosylprotein Kex2
show the reaction diagram
-
PMT4, not PMT1-3
-
-
-
dolichyl phosphate D-mannose + protein Kex2
dolichyl phosphate + O-D-mannosylprotein Kex2
show the reaction diagram
-
PMT4, not PMT1-3
-
?
dolichyl phosphate D-mannose + protein Kex2
dolichyl phosphate + O-D-mannosylprotein Kex2
show the reaction diagram
-
protein is located in the Golgi apparatus
-
-
-
dolichyl phosphate D-mannose + protein Kre9
dolichyl phosphate + O-D-mannosylprotein Kre9
show the reaction diagram
-
mainly PMT1 and PMT2, not PMT3 and PMT4
-
-
-
dolichyl phosphate D-mannose + protein Kre9
dolichyl phosphate + O-D-mannosylprotein Kre9
show the reaction diagram
-
mainly PMT1 and PMT2, not PMT3 and PMT4
-
?
dolichyl phosphate D-mannose + protein Kre9
dolichyl phosphate + O-D-mannosylprotein Kre9
show the reaction diagram
-
protein is located in the Golgi apparatus
-
-
-
dolichyl phosphate D-mannose + protein Pir2/hsp150
dolichyl phosphate + O-D-mannosylprotein Pir2/hsp150
show the reaction diagram
-
PMT1
-
-
-
dolichyl phosphate D-mannose + protein Pir2/hsp150
dolichyl phosphate + O-D-mannosylprotein Pir2/hsp150
show the reaction diagram
-
PMT1
-
?
dolichyl phosphate D-mannose + protein Pir2/hsp150
dolichyl phosphate + O-D-mannosylprotein Pir2/hsp150
show the reaction diagram
-
PMT1, PMT2, and to some extent PMT4, not PMT3
-
-
-
dolichyl phosphate D-mannose + protein Pir2/hsp150
dolichyl phosphate + O-D-mannosylprotein Pir2/hsp150
show the reaction diagram
-
PMT1, PMT2, and to some extent PMT4, not PMT3
-
?
dolichyl phosphate D-mannose + protein Pir2/hsp150
dolichyl phosphate + O-D-mannosylprotein Pir2/hsp150
show the reaction diagram
-
protein is located in the medium
-
-
-
dolichyl phosphate D-mannose + ribonuclease 2
dolichyl phosphate + ribonuclease 2-D-mannose
show the reaction diagram
-
C-mannosylation activity
-
-
-
dolichyl phosphate D-mannose + ribonuclease 2
dolichyl phosphate + ribonuclease 2-D-mannose
show the reaction diagram
-
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
show the reaction diagram
-
biosynthetic pathway
-
-
-
dolichyl phosphate D-mannose + RSPSPSTQ
dolichyl phosphate + O-D-mannosyl-RSPSPSTQ
show the reaction diagram
-
-
-
?
dolichyl phosphate D-mannose + Tyr-Ala-Thr-Ala-Val
dolichyl phosphate + O-D-mannosyl-Tyr-Ala-Thr-Ala-Val
show the reaction diagram
-
-
-
?
dolichyl phosphate D-mannose + Tyr-Ala-Thr-Ala-Val
dolichyl phosphate + O-D-mannosyl-Tyr-Ala-Thr-Ala-Val
show the reaction diagram
P33775, P42934, P52867, Q06644
wild-type and mutants
-
?
dolichyl phosphate D-mannose + Tyr-Asn-Leu-Thr-Ser-Val
dolichyl phosphate + O-D-mannosyl-Tyr-Asn-Leu-Thr-Ser-Val
show the reaction diagram
-
-
-
?
dolichyl phosphate D-mannose + Tyr-Asn-Pro-Thr-Ser-Val
dolichyl phosphate + O-D-mannosyl-Tyr-Asn-Pro-Thr-Ser-Val
show the reaction diagram
-
-
-
?
dolichyl phosphate D-mannose + Tyr-Asn-Pro-Thr-Ser-Val
dolichyl phosphate + O-D-mannosyl-Tyr-Asn-Pro-Thr-Ser-Val
show the reaction diagram
-
-
-
?
dolichyl phosphate D-mannose + Tyr-Asn-Pro-Thr-Ser-Val
dolichyl phosphate + O-D-mannosyl-Tyr-Asn-Pro-Thr-Ser-Val
show the reaction diagram
-
-
-
?
dolichyl phosphate D-mannose + Tyr-Asn-Pro-Thr-Ser-Val
dolichyl phosphate + O-D-mannosyl-Tyr-Asn-Pro-Thr-Ser-Val
show the reaction diagram
-
-
-
?
dolichyl phosphate D-mannose + Tyr-Asn-Pro-Thr-Ser-Val
dolichyl phosphate + O-D-mannosyl-Tyr-Asn-Pro-Thr-Ser-Val
show the reaction diagram
Candida albicans 2005 E
-
-
-
?
dolichyl phosphate D-mannose + Tyr-Asn-Pro-Thr-Ser-Val-NH2
dolichyl phosphate + O-alpha-D-mannosyl-Tyr-Asn-Pro-Thr-Ser-Val-NH2
show the reaction diagram
-
-
-
?
dolichyl phosphate D-mannose + Tyr-Leu-Thr-Ala-Val
dolichyl phosphate + O-D-mannosyl-Tyr-Leu-Thr-Ala-Val
show the reaction diagram
-
-
-
?
dolichyl phosphate D-mannose + Tyr-Pro-Thr-Ala-Val
dolichyl phosphate + O-D-mannosyl-Tyr-Pro-Thr-Ala-Val
show the reaction diagram
-
-
-
?
additional information
?
-
P46971, P47190, -
-
-
-
-
additional information
?
-
-
PMT3: no clearly determined dolichyl-phosphate-mannose-protein mannosyltransferase activity, PMT4 and PMT6 probably function as an active dimer
-
-
-
additional information
?
-
-
PMT1 and PMT2 function as a complex
-
-
-
additional information
?
-
P46971, P47190, -
PMT3 behaves as a dolichyl-phosphate-mannose-glycolipid alpha-mannosyltransferase, EC 2.4.1.130
-
-
-
additional information
?
-
-
defective mutants are used to investigate the substrate specificities of PMT1-4,6 in vivo
-
-
-
additional information
?
-
-
PMT2 is essential for growth, PMT4 is required for full virulence of Candida albicans, PMT5 does not make a significant contribution to virulence
-
-
-
additional information
?
-
-, O74189, Q59X23, Q5ADM9, Q9UVB5
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
-
-
-
additional information
?
-
-
protein O-mannosyltransferase isoforms regulate biofilm formation in Candida albicans
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
Q6R3M9
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
-
-
-
additional information
?
-
-
O-mannosylation of specific secretory proteins of the bacterial pathogen Mycobacterium tuberculosis contributes significantly to virulence
-
-
-
additional information
?
-
Q59X23, Q5ACU3, Q5ADM9
O-mannosylation of specific secretory proteins of the human fungal pathogen Candida albicans contributes significantly to virulence
-
-
-
additional information
?
-
Q59X23, Q5ACU3, Q5ADM9
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
-
-
-
additional information
?
-
-
protein O-mannosyltransferases 1 and 2 are required to maintain integrity of Drosophila larval muscles
-
-
-
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
dolichyl phosphate D-mannose + alpha-dystroglycan
dolichyl phosphate + O-D-mannosyl-[alpha-dystroglycan]
show the reaction diagram
-
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 + glucoamylase I
dolichyl phosphate + O-D-mannosyl glucoamylase I
show the reaction diagram
-, Q96VV1
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 + protein
dolichyl phosphate + O-D-mannosylprotein
show the reaction diagram
-
-
-
-
-
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
show the reaction diagram
P31382, -
-
-
-
-
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
show the reaction diagram
-
-
-
-
-
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
show the reaction diagram
-
-
-
-
-
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
show the reaction diagram
Q5KAF1, Q5KHK5, Q5KIZ1
-
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
show the reaction diagram
-
-
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
show the reaction diagram
-
acceptor substrate specificities of PMT1-4,6
-
-
-
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
show the reaction diagram
P33775, P42934, P52867, Q06644
acceptor substrates: secretory proteins
-
-
-
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
show the reaction diagram
-
production of cell-wall mannoproteins
-
-
-
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
show the reaction diagram
P46971, P47190, -
production of cell-wall mannoproteins
-
-
-
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
show the reaction diagram
-
production of cell-wall mannoproteins
-
-
-
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
show the reaction diagram
-
production of cell-wall mannoproteins
-
-
-
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
show the reaction diagram
P33775, P42934, P52867, Q06644
production of cell-wall mannoproteins
-
-
-
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
show the reaction diagram
-
catalyzes the initial step of O-mannosyl glycan biosynthesis
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
show the reaction diagram
A3E242, -
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
show the reaction diagram
O13898, O42933, Q9C100, -
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
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
show the reaction diagram
O13898, O42933, Q9C100, -
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
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
show the reaction diagram
O13898, O42933, Q9C100, -
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
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
show the reaction diagram
-
protein O-mannosylation is crucial for cell wall integrity, septation and viability
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
show the reaction diagram
-, Q66VU5
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
show the reaction diagram
Candida albicans 2005 E
-
production of cell-wall mannoproteins
-
-
-
dolichyl phosphate D-mannose + protein Aga2
dolichyl phosphate + O-D-mannosylprotein Aga2
show the reaction diagram
-
i.e. small-agglutinin, activity is not affected by disruption mutations of PMT1-4, protein is located at the cell surface
-
-
-
dolichyl phosphate D-mannose + protein AN5660
dolichyl phosphate + O-D-mannosylprotein
show the reaction diagram
Q5B3W9, Q5BDC1, Q96WN5
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 Bar1
dolichyl phosphate + O-D-mannosylprotein Bar1
show the reaction diagram
-
PMT1 and PMT2, not PMT3 and PMT4, protein is located in the medium
-
-
-
dolichyl phosphate D-mannose + protein chitinase 1
dolichyl phosphate + O-D-mannosylprotein chitinase 1
show the reaction diagram
-
PMT1
-
-
-
dolichyl phosphate D-mannose + protein chitinase 1
dolichyl phosphate + O-D-mannosylprotein chitinase 1
show the reaction diagram
-
PMT1, PMT4, PMT6 and especially PMT2, not PMT3, protein is located in the cell wall and medium
-
-
-
dolichyl phosphate D-mannose + protein Ggp1/Gas1
dolichyl phosphate + O-D-mannosylprotein Ggp1/Gas1
show the reaction diagram
-
PMT4 and PMT6, not PMT1-3, protein is located at the cell surface
-
-
-
dolichyl phosphate D-mannose + protein Kex2
dolichyl phosphate + O-D-mannosylprotein Kex2
show the reaction diagram
-
PMT4, not PMT1-3, protein is located in the Golgi apparatus
-
-
-
dolichyl phosphate D-mannose + protein Kre9
dolichyl phosphate + O-D-mannosylprotein Kre9
show the reaction diagram
-
mainly PMT1 and PMT2, not PMT3 and PMT4, protein is located in the Golgi apparatus
-
-
-
dolichyl phosphate D-mannose + protein Pir2/hsp150
dolichyl phosphate + O-D-mannosylprotein Pir2/hsp150
show the reaction diagram
-
PMT1
-
-
-
dolichyl phosphate D-mannose + protein Pir2/hsp150
dolichyl phosphate + O-D-mannosylprotein Pir2/hsp150
show the reaction diagram
-
PMT1, PMT2, and to some extent PMT4, not PMT3, protein is located in the medium
-
-
-
dolichyl phosphate D-mannose + ribonuclease 2
dolichyl phosphate + ribonuclease 2-D-mannose
show the reaction diagram
-
C-mannosylation activity, biosynthetic pathway
-
-
-
additional information
?
-
-
defective mutants are used to investigate the substrate specificities of PMT1-4,6 in vivo
-
-
-
additional information
?
-
-
PMT2 is essential for growth, PMT4 is required for full virulence of Candida albicans, PMT5 does not make a significant contribution to virulence
-
-
-
additional information
?
-
-, O74189, Q59X23, Q5ADM9, Q9UVB5
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
-
-
-
additional information
?
-
-
protein O-mannosyltransferase isoforms regulate biofilm formation in Candida albicans
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
Q6R3M9
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
-
-
-
additional information
?
-
-
O-mannosylation of specific secretory proteins of the bacterial pathogen Mycobacterium tuberculosis contributes significantly to virulence
-
-
-
additional information
?
-
Q59X23, Q5ACU3, Q5ADM9
O-mannosylation of specific secretory proteins of the human fungal pathogen Candida albicans contributes significantly to virulence
-
-
-
additional information
?
-
Q59X23, Q5ACU3, Q5ADM9
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
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Mg2+
-
Mg2+ or Mn2+ stimulates; optimal stimulation at 7 mM
Mg2+
-
not required
Mg2+
-
2fold activation
Mg2+
-
required, 10 mM
Mn2+
-
Mg2+ or Mn2+ stimulates
additional information
-
at 0.5 M KCl pmt4 mutant grows slower than wild-type, at 0.7 M growth inhibition; at 1 M MaCl growth inhibition of mutant pmt1 but to a lesser extent than mutant pmt4; at 1 M NaCl growth inhibition of mutant pmt4
additional information
Q5KAF1, Q5KHK5, Q5KIZ1
at 0.5 M KCl pmt4 mutant grows slower than wild-type, at 0.7 M growth inhibition; at 1 M NaCl growth inhibition of mutant pmt1 but to a lesser extent than mutant pmt4; at 1 M NaCl growth inhibition of mutant pmt4
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
Chymotrypsin
-
inactivation
-
CuSO4
-
10 mM, complete inhibition
glycerol
-
at 20% inhibitory
glycerol
-
at 50% inhibitory
Mg2+
-
above 5 mM
phosphatidylinositol
-
-
additional information
-
not affected by Triton X-100 up to 0.2%
-
additional information
-
no inhibition by EDTA
-
additional information
-
not inhibitory: Mg2+, Mn2+, Ca2+
-
additional information
-
cell wall destabilizing agents Congo red, caffeine, and calcofluor white have no effect on the growth of any pmt mutants
-
additional information
Q5KAF1, Q5KHK5, Q5KIZ1
cell wall destabilizing agents Congo red, caffeine, and calcofluor white have no effect on the growth of any pmt mutants; cell wall destabilizing agents Congo red, caffeine, and calcofluor white have no effect on the growth of any pmt mutants
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
deoxycholate
-
0.025%, stimulates slightly
phosphatidylcholine
-
stimulates
phosphatidylglycerol
-
-
phosphatidylinositol
-
-
EDTA
-
up to 3fold stimulation
additional information
-
not affected by Triton X-100 up to 0.2%
-
additional information
-
no effect: Mn2+, Mg2+, Ca2+
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
6.7
-
Ac-Ala-Thr-Ala-NH2
-
-
0.25
-
Ac-Tyr-Ala-Thr-Ala-Val-NH2
-
-
2
-
Ac-Tyr-Ala-Thr-Ala-Val-NH2
-
PMT1
15
-
Ac-Tyr-Ala-Thr-Ala-Val-NH2
-
additional enzyme form
4.3
-
Ac-Tyr-Asn-Pro-Thr-Ser-Val-NH2
-
-
0.1
-
biotin-Tyr-Leu-Ala-Val-NH2
-
-
0.85
-
biotin-Tyr-Pro-Thr-Ala-Val-NH2
-
-
0.075
-
biotin-Tyr-Thr-Ala-Val-NH2
-
-
10
-
RSPSPSTQ
-
additional enzyme form
-
20
-
RSPSPSTQ
-
PMT1
-
0.63
-
synthetic peptide based on a mucin-like domain in alpha-dystroglycan
-
25C, pH 8.0
-
0.73
-
synthetic peptide based on a mucin-like domain in alpha-dystroglycan
-
25C, pH 8.0
-
2.96
-
synthetic peptide based on a mucin-like domain in alpha-dystroglycan
-
25C, pH 8.0
-
2.98
-
synthetic peptide based on a mucin-like domain in alpha-dystroglycan
-
25C, pH 8.0
-
9.7
-
synthetic peptide based on a mucin-like domain in alpha-dystroglycan
-
25C, pH 8.0
-
2.2
-
Tyr-Ala-Thr-Ala-Val
-
-
1
-
Tyr-Asn-Pro-Thr-Ser-Val
-
-
3.3
-
Tyr-Asn-Pro-Thr-Ser-Val
-
-
2.5
-
Tyr-Leu-Thr-Ala-Val
-
-
7.3
-
Tyr-Pro-Thr-Ala-Val
-
-
0.4
-
dolichyl phosphate D-mannose
-
-
additional information
-
additional information
-
Km value depends on chain length and alpha-saturation of the acceptor substrate
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.0000012
-
-
substrate YNPTSV
0.0000677
-
-
partially purified enzyme
0.00057
-
-
partially purified enzyme
0.0035
-
-
partially purified enzyme
additional information
-
-
-
additional information
-
-
specific activity of the additional enzyme form is 7fold higher than that of PMT1, substrate Ac-YNPTSV-NH2
additional information
-
-
-
additional information
-
-
-
additional information
-
-
wild-type and deletion mutants
additional information
-
-
assay development on microtiter plates
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.5
-
-
PMT1 null mutant, optimum of the additional enzyme form
6.5
-
-
assay at
7.2
-
-
assay at
7.5
8
-
the best buffers are bicine pH 7.7, tricine pH 8.0 and HEPES pH 7.5
7.5
-
-
assay at
7.5
-
-
PMT1 wild-type
7.5
-
-
assay at
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
22
-
-
additional enzyme form
25
-
-
assay at
26
-
-
about
37
-
-
assay at
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
28
37
-
in vivo
additional information
-
-
40% remaining activity at 0C
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
Q14U74, Q99PR0
Pomt1 and Pomt2 mRNA are coexpressed in neurons (dentate gyrus and CA1-CA3 region of the hippocampus and cerebellar Purkinje cells); Pomt1 and Pomt2 mRNA are coexpressed in neurons (dentate gyrus and CA1-CA3 region of the hippocampus and cerebellar Purkinje cells)
Manually annotated by BRENDA team
-
sPomt2, but not tPomt2, is prominently expressed in mouse embryos in the tissues that are most severely affected in Walker-Warburg syndrome (developing muscle, eye, and brain)
Manually annotated by BRENDA team
-
tPOMT2 is restricted to the acrosome of male germ cells and is not involved in the biosynthesis of O-mannosyl glycans in vivo. tPOMT2 is highly conserved among mammals, including humans, suggesting a crucial function that is distinct from sPOMT2
Manually annotated by BRENDA team
-
of brain with subarachnoid spread. Distinct POMT1 alterations may contribute to a functional impairment of protein-omannosyltransferase activity. In individual tumor specimens selective alterations of the POMT1 gene may be compatible with clonal evolution of distinct sublocations
Manually annotated by BRENDA team
Q14U74, Q99PR0
;
Manually annotated by BRENDA team
-
human embryonic kidney
Manually annotated by BRENDA team
Q14U74, Q99PR0
;
Manually annotated by BRENDA team
-
highest activity
Manually annotated by BRENDA team
Q14U74, Q99PR0
;
Manually annotated by BRENDA team
Q14U74, Q99PR0
;
Manually annotated by BRENDA team
-
lymphoblast-based enzymatic assays are accurate and useful methods to select patients harbouring POMT1 and POMT2 mutations among those with a suspected or confirmed alpha-dystroglycanopathy; lymphoblast-based enzymatic assays are accurate and useful methods to select patients harbouring POMT1 and POMT2 mutations among those with a suspected or confirmed alpha-dystroglycanopathy
Manually annotated by BRENDA team
-
with subarachnoid spread. Distinct POMT1 alterations may contribute to a functional impairment of protein-O-mannosyltransferase activity. In individual tumor specimens selective alterations of the POMT1 gene may be compatible with clonal evolution of distinct sublocations
Manually annotated by BRENDA team
-
lowest activity
Manually annotated by BRENDA team
-
lowest expression
Manually annotated by BRENDA team
Q14U74, Q99PR0
Pomt1 is most strongly expressed in testis; Pomt2 is most strongly expressed in testis
Manually annotated by BRENDA team
-
in testis both POMT2 isoforms are stably expressed. In contrast to tPOMT2, which is restricted to developing spermatogenic cells, sPOMT2 is present in nonspermatogenic cells. sPOMT2POMT1 complexes catalyze mannosyltransfer in adult somatic tissues and testis
Manually annotated by BRENDA team
-
highest expression
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
many proteins are O-mannosylated inside the endoplasmic reticulum by an O-mannosyltransferase, the Pmt1p-Pmt2p complex
Manually annotated by BRENDA team
-
integral, multiple transmembranal domains; integral, multiple transmembranal domains
Manually annotated by BRENDA team
-
integral, multiple transmembranal domains
Manually annotated by BRENDA team
-
a membrane protein
Manually annotated by BRENDA team
Candida albicans 2005 E, Saccharomyces cerevisiae BY4743
-
-
-
Manually annotated by BRENDA team
Candida albicans 2005 E
-
-
-
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
71000
-
Q9Y6A1
limb girdle muscular dystrophy deletion mutant p.A589VfsX38 enzyme, Western blot analysis, SDS-PAGE with antibody staining
73000
-
-
rough estimate from SDS-PAGE figure, fully glycosylated enzyme, 2-3 kDa lower than wild-type corresponds to lack of a single N-glycan chain
85000
-
Q9Y6A1
limb girdle muscular dystrophy mutant L171A enzyme, Western blot analysis, SDS-PAGE with antibody staining; wild-type enzyme, Western blot analysis, SDS-PAGE with antibody staining
88200
-
-
AnPmtC, calculated from amino acid sequence
103300
-
-
AnPmtB, calculated from amino acid sequence
additional information
-
Q9Y6A1
Walker-Warburg syndrome p.del77-93 mutant enzyme is not detectable, Western blot analysis, SDS-PAGE with antibody staining
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 92000, PMT1, SDS-PAGE; x * 92000, SDS-PAGE
?
-
x * 78000, PMT2, SDS-PAGE; x * 92000, PMT1, SDS-PAGE
?
-
x * 70000, SDS-PAGE
?
-
x * 88000, Pmt2p
heterodimer
-
AnpmtB with AnpmtA, 2 * ?; AnpmtB with AnpmtA, but AnPmtB disruption mutant shows different phenotype than AnpmtA disruptant, independent function
homodimer
-
-
additional information
-
PMT1 and PMT2 function as a complex
additional information
-
PMT1 and PMT2 function as a complex; PMT4 and PMT6 probably function as an active dimer
additional information
-
Arg138 is crucial for complex formation between PMT1 and PMT2, N-terminal third of the protein is essential for complex formation; central hydrophilic loop is essential for catalytic activity, not complex formation, and is conserved throughout the PMT-family; PMT1 and PMT2 function as a complex; topology model of PMT1
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
glycoprotein
-
POMT1, 3 of 4 potential glycosylation sites, inhibition of glycosylation with tunicamycin inactivates enzyme, mutation of all sites prevents solubilization of the enzyme; POMT2, all of 5 potential glycosylation sites, inhibition of glycosylation with tunicamycin inactivates enzyme, mutation of all sites prevents solubilization of the enzyme; three of the four POMT1 sites (Asn435, Asn471 and Asn539) and all five of the POMT2 N-glycosylation sites (Asn98, Asn330, Asn445, Asn528 and Asn583) are N-glycosylated
glycoprotein
-
may contain 4 carbohydrate chains
glycoprotein
-
PMT1 and PMT2 contain both 3 putative N-glycosylation sites; PMT1 and PMT2 contain both 3 putative N-glycosylation sites
glycoprotein
-
construction of diverse deletion mutants with different numbers of N-glycosylation sites; PMT1: 3 N-glycosylation sites
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4.9
-
-
inactivation below pH 4.9
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
26
-
-
22 h, stable
37
-
-
60 min, stable
95
-
-
inactivation
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
stable in solution with deoxycholate and CHAPS
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-80C, partially purified enzyme, indefinitely stable
-
23C, partially purified enzyme, 2% glycerol, at least 12 h stable
-
4-23C, partially purified enzyme, stable for at least 1 week
-
4C, solubilized with 0.5% Triton X-100, loss of 80% activity within 5 days
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
gel purification of disruption mutants
-
gel purification of disruption mutants; gel purification of disruption mutants; gel purification of disruption mutants
Q5KAF1, Q5KHK5, Q5KIZ1
conidia are incubated, filtered and washed with stop buffer (pH 7.0), ground in liquid nitrogen, centrifuged, supernatant centrifuged, pellet with crude membranes resuspended, resolved by SDS-PAGE, immunodetection of target protein AN5660; conidia are incubated, filtered and washed with stop buffer (pH 7.0), ground in liquid nitrogen, centrifuged, supernatant centrifuged, pellet with crude membranes resuspended, resolved by SDS-PAGE, immunodetection of target protein AN5660; conidia are incubated, filtered and washed with stop buffer (pH 7.0), ground in liquid nitrogen, centrifuged, supernatant centrifuged, pellet with crude membranes resuspended, resolved by SDS-PAGE, immunodetection of target protein AN5660
Q5B3W9, Q5BDC1, Q96WN5
glutathione-Sepharose 4B bead chromatography; isolation of microsome fraction: cells are homogenized in 10 mM Tris-HCl, pH 7.4, EDTA, sucrose, DTT, protease inhibitors, centrifugation, supernatant ultracentrifuged, precipitate used as microsomal fraction, solubilized in 20 mM Tris-HCl, pH 8.0, 2-mercaptoethanol, EDTA, n-octyl-beta-D-thioglucoside, centrifugation, supernatant used as solubilized microsome preparation, separation with SDS-PAGE and antibody staining
-
glutathione-Sepharose column chromatography
-
glutathione Sepharose column chromatography
-
IgG-coupled magnetic bead chromatography
-
immunoaffinity chromatography, co-purification of PMT1 and PMT2 as a complex, no immuno-cross reactivity
-
partial; solubilization with 0.5% deoxycholate and 1.2% CHAPS
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression of Pmt4 in a Saccharomyces cerevisiae pmt1pmt4 mutant strain functionally complements the deficient Pmt activity
A3E242, -
PCR-amplification of reference strain open reading frames cloned into standard cloning vectors, expressed in fungus
-
PCR-amplification of reference strain open reading frames cloned into standard cloning vectors, expressed in fungus; PCR-amplification of reference strain open reading frames cloned into standard cloning vectors, expressed in fungus; PCR-amplification of reference strain open reading frames cloned into standard cloning vectors, expressed in fungus
Q5KAF1, Q5KHK5, Q5KIZ1
PCR amplification, creation of fusion enzymes with replacement cassettes; PCR amplification, creation of fusion enzymes with replacement cassettes; PCR amplification, creation of fusion enzymes with replacement cassettes
Q5B3W9, Q5BDC1, Q96WN5
PCR-amplification, introduction of replacement cassettes to disrupt genes
-
expressed in HEK-293T cells
-
expressed in HEK-293T cells; transfection of expression plasmids with wild-type and mutant enzyme variants into HEK-293T cells
-
PCR-amplification of blood derived enzyme gene
Q9Y6A1
expressed in Escherichia coli OrigamiTM (DE 3) cells
-
;
Q14U74, Q99PR0
;
P33775, P42934, P52867, Q06644
; DNA sequence determination
-
chromosome mapping of PMT1; DNA sequence determination, chromosome mapping
-
cloning and overexpression of PMT2 in yeast strain GFUII-4B, showing no alteration of enzyme activity, and co-overexpression with PMT1 in yeast strain TF1.8, leading to 3fold increase in enzyme activity in vitro, thus PMT1 and 2 function as a complex
-
expression in Saccharomyces cerevisiae; expression in Saccharomyces cerevisiae; expression in Saccharomyces cerevisiae
-
PCR-amplification to create mutants, full gene transfer via expression vector to Schizosaccharomyces pombe (deficient in pmt) for complementation studies; PCR-amplification to create mutants, full gene transfer via expression vector to Schizosaccharomyces pombe (deficient in pmt) for complementation studies; PCR-amplification to create mutants, full gene transfer via expression vector to Schizosaccharomyces pombe (deficient in pmt) for complementation studies
Q4P140, Q4P339, Q4P380
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
no change in expression of either isoform upon growth in nutrient rich medium at 30 and 37C, with additional salt stress or under capsule-inducing conditions, expression is not unregulated due to deficiency in one other isoform
-
no change in expression of either isoform upon growth in nutrient rich medium at 30 and 37C, with additional salt stress or under capsule-inducing conditions, expression is not unregulated due to deficiency in one other isoform; no change in expression of either isoform upon growth in nutrient rich medium at 30 and 37C, with additional salt stress or under capsule-inducing conditions, expression is not unregulated due to deficiency in one other isoform; no change in expression of either isoform upon growth in nutrient rich medium at 30 and 37C, with additional salt stress or under capsule-inducing conditions, expression is not unregulated due to deficiency in one other isoform
Q5KAF1, Q5KHK5, Q5KIZ1
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
D77A
-
the PMT1 mutant shows 71.95% activity compared to the wild type enzyme
D77A/E78A
-
the PMT1 mutant shows 0.19% activity compared to the wild type enzyme; the PMT1 mutant shows 3.59% activity compared to the wild type enzyme
D77A/E78A/D92A/E93A
-
the PMT1/PMT2 mutant shows 0.24% activity compared to the wild type enzyme
D80A
-
the PMT4 mutant shows 3.21% activity compared to the wild type enzyme
D80E
-
the PMT4 mutant shows 52.98% activity compared to the wild type enzyme
D80E/E81D
-
the PMT4 mutant shows 116.54% activity compared to the wild type enzyme
D92A/E93A
-
the PMT2 mutant shows 3.63% activity compared to the wild type enzyme
D96A
-
the PMT1 mutant shows 63.21% activity compared to the wild type enzyme
E44A
-
inactive
E78A
-
the PMT1 mutant shows 46.68% activity compared to the wild type enzyme
E81A
-
the PMT4 mutant shows 1.43% activity compared to the wild type enzyme
E81D
-
the PMT4 mutant shows 46.59% activity compared to the wild type enzyme
E86A
-
the mutant shows about 70% activity compared to the wild type enzyme
F76A
-
the PMT1 mutant shows 78.79% activity compared to the wild type enzyme
F81A
-
the PMT1 mutant shows 71.71% activity compared to the wild type enzyme
H80A
-
the PMT1 mutant shows 83.03% activity compared to the wild type enzyme
H98A
-
the PMT1 mutant shows 62.77% activity compared to the wild type enzyme
N16Q
-
not smaller than wild-type, may be too close to membrane for a glycosylation site, single mutation with about 70% of wild-type activity; the mutant shows a lower enzymatic activity to about 70% of wild type
N16Q/N435Q/N471Q/N539Q
-
together with POMT2 mutant N98Q/N330Q/N445Q/N528Q/N583Q, significantly lower activity than double wild-type, a lack of glycosylation prevents solubilization; together with wild-type POMT2, significantly lower activity than double wild-type, a lack of glycosylation prevents solubilization
N330Q
-
2-3 kDa smaller than wild-type corresponding to single N-glycan chain, single mutation with no effect on activity
N435Q
-
2-3 kDa smaller than wild-type corresponding to single N-glycan chain, single mutation with about 70% of wild-type activity; the mutant shows about wild type activity; the mutant shows a lower enzymatic activity to about 70% of wild type
N445Q
-
2-3 kDa smaller than wild-type corresponding to single N-glycan chain, single mutation with no effect on activity; the mutant shows about wild type activity
N471Q
-
2-3 kDa smaller than wild-type corresponding to single N-glycan chain, single mutation with about 70% of wild-type activity; the mutant shows a lower enzymatic activity to about 70% of wild type
N528Q
-
2-3 kDa smaller than wild-type corresponding to single N-glycan chain, single mutation with no effect on activity; the mutant shows about wild type activity
N539Q
-
2-3 kDa smaller than wild-type corresponding to single N-glycan chain, single mutation with no effect on activity; the mutant shows about wild type activity
N583Q
-
2-3 kDa smaller than wild-type corresponding to single N-glycan chain, single mutation with no effect on activity; the mutant shows about wild type activity
N98Q
-
2-3 kDa smaller than wild-type corresponding to single N-glycan chain, single mutation with about 50% of wild-type activity; the mutant shows a lower enzymatic activity to about 50% of wild type
N98Q/N330Q/N445Q/N528Q/N583Q
-
together with POMT1 mutant N16Q/N435Q/N471Q/N539Q, significantly lower activity than double wild-type, a lack of glycosylation prevents solubilization; together with wild-type POMT1, significantly lower activity than double wild-type, a lack of glycosylation prevents solubilization
P100A
-
the PMT1 mutant shows 59.67% activity compared to the wild type enzyme
P99A
-
the PMT1 mutant shows 61.77% activity compared to the wild type enzyme
R105A
-
inactive
R145A
-
the mutant shows about 130% activity compared to the wild type enzyme
R30A
-
the mutant shows less than 10% activity compared to the wild type enzyme
R72A
-
the mutant shows about 65% activity compared to the wild type enzyme
V97A
-
the PMT1 mutant shows 80.23% activity compared to the wild type enzyme
Y88A
-
the PMT1 mutant shows 73.79% activity compared to the wild type enzyme
D96A
-
site-directed mutagenesis, exchange of conserved residue in the central loop, reduced activity
E78A
-
site-directed mutagenesis, exchange of conserved residue in the central loop, highly reduced activity
H346A/H348A
-
site-directed mutagenesis, exchange of conserved residue in the central loop, reduced activity
H411A
-
site-directed mutagenesis, exchange of conserved residue in the central loop, slightly reduced activity
H472A
-
site-directed mutagenesis, exchange of conserved residue in the central loop, reduced activity
K234A
-
site-directed mutagenesis, exchange of conserved residue in the central loop, slightly reduced activity
L399A
-
site-directed mutagenesis, exchange of conserved residue in the central loop, reduced activity
L408A
-
site-directed mutagenesis, exchange of conserved residue in the central loop, highly reduced activity
N370A
-
site-directed mutagenesis, exchange of conserved residue in the central loop, slightly reduced activity
Q359A/Q360A
-
site-directed mutagenesis, exchange of conserved residue in the central loop, reduced activity
Q493A/E495A
-
site-directed mutagenesis, exchange of conserved residue in the central loop, reduced activity
R138A
-
site-directed mutagenesis, exchange of conserved residue in the central loop, highly reduced activity
R398A
-
site-directed mutagenesis, exchange of conserved residue in the central loop, reduced activity
R469A
-
site-directed mutagenesis, exchange of conserved residue in the central loop, slightly reduced activity
R64 A
-
site-directed mutagenesis, exchange of conserved residue in the central loop, highly reduced activity
additional information
-
disruption after amino acid D439 results in pmt1A lacking mutants are viable but show distinct defects in cell morphology and cell integrity (wild-type comparable growth at 30C, reduced growth at 37C, no growth at 39C in contrast to wild-type, more susceptible to SDS medium, enlarged cells subject to spontaneous lysis, attenuated virulence), Pmt1/Pmt4 double mutants are not viable, pmt1A mutant is susceptible to sorbitol (2.5 M) and to 0.1% SDS, reduced survival upon macrophage attack; disruption after amino acid E468 results in pmt2A lacking mutants, not viable, one wild-type allele is necessary for growth, after sporulation no haploid pmt2 lacking mutants are found, Pmt2 is essential but an intact Pmt2 gene lacking the other two isoforms is not sufficient for viability, may be due to interaction with the other isoforms; disruption after amino acid K461 results in pmt4A lacking mutants, viable but with distinct defects in cell morphology and cell integrity (wild-type comparable growth at 30C, reduced growth at 37C, no growth at 39C in contrast to wild-type, poor growth on high salt medium, abnormal septum formation, enlarged cells subject to spontaneous lysis, multi-cell aggregate formation based on defects in cell separation, delayed melanin production, slightly reduced capsule size, attenuated virulence), Pmt1/Pmt4 double mutants are not viable, points to necessary interaction with the Pmt2 isoform or essential combined target, the pmt4A mutant is susceptible to sorbitol (2 M), reduced survival upon macrophage attack
additional information
Q5KAF1, Q5KHK5, Q5KIZ1
disruption after amino acid N508 results in pmt2D lacking mutants, not viable, one wild-type allele is necessary for growth, after sporulation no haploid pmt2 lacking mutants are found, Pmt2 is essential but an intact Pmt2 gene lacking the other two isoforms is not sufficient for viability may be due to interaction with the other isoforms; disruption after amino acid Q412 results in pmt4D lacking mutants, aviable but with distinct defects in cell morphology and cell integrity (wild-type comparable growth at 30C, reduced growth at 37C, no growth at 39C in contrast to wild-type, poor growth on high salt medium, abnormal septum formation, enlarged cells subject to spontaneous lysis, multi-cell aggregate formation based on defects in cell separation, delayed melanin production, slightly reduced capsule size, attenuated virulence), Pmt1/Pmt4 double mutants are not viable, points to necessary interaction with the Pmt2 isoform or essential combined target, the pmt4D strain is not inhibited by sorbitol but is inhibited by SDS, bilateral crossing of two pmt4D mutant strains delays mating reaction with reduced filament formation, less aerial hyphae, irregular shape and thickness of filaments with swollen distal tips; disruption after amino acid W315 results in pmt1D lacking mutants are viable but show distinct defects in cell morphology and cell integrity (wild-type comparable growth at 30C, reduced growth at 37C, no growth at 39C in contrast to wild-type, more susceptible to SDS medium, enlarged cells subject to spontaneous lysis, attenuated virulence), Pmt1/Pmt4 double mutants are not viable, the pmt1D mutant grows poorly in sorbitol, is unaffected by SDS, no defects in mating and crossing are observed
additional information
-
mutants lacking or overexpressing one of the two or both O-mannosyltransferases Rotated Abdomen and Twisted show that both are required for in vivo production of high molecular mass dystroglycan, overexpression of only one isoform does not increase its amount over wild-type, lack of either one of the isoforms or both isoforms lacking double mutant do not produce the high molecular mass dystroglycan
yes
-
mutants lacking or overexpressing one of the two or both O-mannosyltransferases Rotated Abdomen and Twisted show that both are required for in vivo production of high molecular mass dystroglycan, overexpression of only one isoform does not increase its amount over wild-type, lack of either one of the isoforms or both isoforms lacking double mutant do not produce the high molecular mass dystroglycan
additional information
-
enzyme disruption mutant, 6% of wild-type activity, underglycosylation of an extracellular glucoamylase. Disruption mutant shows abnormal cell morphology and alteration in carbohydrate composition, reduction n the skeletal polysaccharides in the cell wall
additional information
-
Anpmta + AnpmtB double disruptant is viable but very slow growing with morphological characteristics (swollen hyphae with ballon structures + hyperbranched hyphae) cumulative of single disruptants at 30 and 42C, partial improvement of defects by addition of osmotic stabilizer; AnpmtA disruptant, increased sensitivity to hygromycin B (increased cell wall permeability), glycoprotetin profile (plasma membrane proteins) almost indistinguishable from wild-type, underglycosylation of protein AN5660 upon AnpmtC diruption; AnPmtB disruptant shows wild-type colony formation at 30C, slightly repressed growth at 42C, the osmotic stabilizer 0.6 M KCl reduces these effects, conidiation reduced to about 56%, swollen vesicles, hyperbranching of hyphae (defect in polarity maintenance), underglycosylation of glucoamylase I upon gene disruption, higher sensitivity to inhibitors of cell wall synthesis (beta-glucan and beta-1,3-glucan production) congo red and micafungin, not to calcofluor (inhibiting chitin synthesis), no increased sensitivity to hygromycin B, glycoproetin profile (plasma membrane proteins) almost indistinguishable from wild-type, underglycosylation of glucoamylase I upon AnpmtB diruption; AnpmtC disruptant with highest growth repression, swollen, frequently branched hyphae, strongly reduced conidia formation (6% of wild-type), recovery of hyphal structures in the presence of osmotic stabilizers (0.6 M KCl, 0.8 M NaCl, or 1.2 M sorbitol) at 42C, enables conidiophore and conidia production (abnormal and fewer), underglycosylation of glucoamylase I upon gene diruption, higher sensitivity to inhibitors of cell wall synthesis (beta-glucan and beta-1,3-glucan production) congo red and micafungin, not to calcofluor (inhibiting chitin synthesis), more sensitive to hygromycin B than wild-type, increase of 65 kDa proteins, of mannose-containing glycoproteins (plasma membrane proteins) of about 80 kDa, reduced number of proteins larger than 100 kDa and of 75 kDa, underglycosylation of glucoamylase I and of protein AN5660 upon AnpmtC diruption
additional information
Q5B3W9, Q5BDC1, Q96WN5
at 25 and 30C normal growth of single deletion mutants, reduced growth at high temperatures (37 and 42C), deltapmtA deletion mutant is more heat sensitive than deltapmtC and deltapmtB, double deletion mutant deltapmtA + deltapmtB is the most heat sensitive, partial restoration of heat tolerance by addition of the osmotic sorbitol, the pmtA deletion mutant is more sensitive to cell wall-perturbing agents Calcofluor and Congo red than the wild-type, at 30C more germ tubes emerge early compared to wild-type and the other deletion mutants except double deletion mutant deltapmtA + deltapmtB, swollen conidia, partial or no conidiogenous layers, at 42C 2 to 3times swollen conidia, no germ tubes, fewer conidia; at 25 and 30C normal growth of single deletion mutants, reduced growth at high temperatures (37 and 42C), double deletion mutant deltapmtA + deltapmtB is the most heat sensitive, deltapmtA deletion mutant is more heat sensitive than deltapmtC and deltapmtB, partial restoration of heat tolerance by addition of the osmotic sorbitol or KCl (not conidial production), the deltapmtC deletion mutant is resistant to Calcofluor at all temperatures but sensitive to Congo red at elevated temperatures, at 30C more multiple germ tubes than in the wild-type and in the other deletion mutants, excessive aerial hyphae, fewer conidiophores on elongated stalks, condigiogenous layers misplaced, at 37C vesicles and conidiogenous layers swollen, fewer spores at all temperatures at 42C swollen germ tubes and hyperbranching; at 25 and 30C normal growth of single deletion mutants, reduced growth at high temperatures (37 and 42C), pmtA deletion mutant is more heat sensitive than deltapmtC and deltapmtB, double deletion mutant deltapmtA + deltapmtB is the most heat sensitive, partial restoration of heat tolerance by addition of the osmotic sorbitol or KCl, at 25C the pmtB deletion mutant grows as well as the wild-type in the presence of cell wall-perturbing agents, at 30 and 37C it is hypersensitive to Calcofluor, at 42C it is resistant to Calcofluor, to Congo red it is hypersensitive at 37 and 42C, resistant at lower temperatures, at 42C lysis of 30% of hyphen tips, at permissive temperature mostly normal conidiophores, occasional lysed vesicles, at restrictive temperature many swollen conidiophore stalks and lysed vesicles, fewer conidia, at 30C hyphae are growing from adjacent compartments into lysed areas forming intrahyphal hyphae; double deletion mutant of pmtA + pmtB is the only viable double mutant, it shows slightly retarded growth even at 25C and is the most heat sensitive deletion mutant, followed in sensitivity by deltapmtA, deltapmtC, and deltapmtB, partial restoration of heat tolerance by addition of the osmotic sorbitol or KCl (not conidial production), the double deletion mutant is more sensitive to cell wall-perturbing agents Calcofluor and Congo red than the wild-type at all tested temperatures, at 25C swollen conidiophore stalks, vesicles, and conidiogenous layers, at 30C more germ tubes emerge early compared to wild-type and the other deletion mutants except deltapmtA, lysis of hyphen tips at permissive temperature, at 37C vegetative and aerial hyphae badly swollen, conidiophores not detectable, reduced conidia productiondefective polar growth at restrictive temperature, at 30C hyphae are growing from adjacent compartments into lysed areas forming intrahyphal hyphae; double deletion mutant of pmtA + pmtB is the only viable double mutant, it shows slightly retarded growth even at 25C and is the most heat sensitive deletion mutant, followed in sensitivity by deltapmtA, deltapmtC, and deltapmtB, partial restoration of heat tolerance by addition of the osmotic sorbitol or KCl (not conidial production), the double deletion mutant is more sensitive to cell wall-perturbing agents Calcofluor and Congo red than the wild-type at all tested temperatures, at 25C swollen conidiophore stalks, vesicles, and conidiogenous layers, at 30C more germ tubes emerge early compared to wild-type and the other deletion mutants except deltapmtA, lysis of hyphen tips at permissive temperature, at 37C vegetative and aerial hyphae badly swollen, conidiophores not detectable, reduced conidia productiondefective polar growth at restrictive temperature, at 30C hyphae are growing from adjacent compartments into lysed areas forming intrahyphal hyphae; double deletion mutant of pmtB + pmtC is not viable; double deletion mutant of pmtB + pmtC is not viable; double deletion mutants of pmtA + pmtC is not viable; double deletion mutants of pmtA + pmtC is not viable; the triple deletion mutant of pmtA + pmtB + pmtC is not viable; the triple deletion mutant of pmtA + pmtB + pmtC is not viable; the triple deletion mutant of pmtA + pmtB + pmtC is not viable
L171A
Q9Y6A1
stable enzyme with reduced activity causing phenotype limb girdle muscular dystrophy 2K, together with partial heterozygous deletion p.A589VfsX38 mutant, reduced amounts of O-mannosyl linked glyco-epitope (IIH6) on alpha-dystroglycans resulting in less than 100-125 kDa alpha-dystroglycans, about 40% residual enzyme activity
additional information
-
mutations of all N-glycosylation sites of either isoform POMT1 or POMT2 cause a loss of enzyme activity; single site mutations defective in potential glycosylation sites do not change enzyme activity, mutaions of all such sites cause a loss of enzyme activity, probably due to decreased hydrophilicity; single site mutations defective in potential glycosylation sites do not change enzyme activity, mutations of all such sites cause a loss of enzyme activity, probably du to decreased hydrophilicity
additional information
Q9Y6A1
heterozygous deletion leading to a frame shift mutation causing an amino acid exchange A589V and a premature stop codon after 38 amino acids (p.A589VfsX38), reduced enzyme stability, reduced amounts of O-mannosyl linked glyco-epitope (IIH6) on alpha-dystroglycans resulting in less than 100-125 kDa alpha-dystroglycans, about 40% residual enzyme activity, phenotype limb girdle muscular dystrophy 2K
L408A/H411A
-
site-directed mutagenesis, exchange of conserved residue in the central loop, highly reduced activity
additional information
-
homozygous diploid double disruption mutants of PMT1 and PMT2 lead to reduced enzyme activity and a severe defect in sporulation, lethal phenotype when combined with a disruption mutation in dolichyl-phosphate-mannose-glycolipid alpha-mannosyltransferase, EC 2.4.1.130, genes; PMT3 and 4 gene disruption does not alter enzyme activity; PMT3 and 4 gene disruption does not alter enzyme activity
additional information
-
PMT1 null mutant shows increased heat lability, alpa-D-mannose transfer only to serine residue of the substrate peptide Ac-YNPTSV-NH2, not to threonine and valine like with the wild-type
additional information
-
PMT1 and PMT2 double disruption mutant shows severe growth defect but retain residual activity due to an additional enzyme; PMT1 and PMT2 double disruption mutant shows severe growth defect but retain residual activity due to an additional enzyme; PMT2 disruption mutant shows reduced in vitro and in vivo activity; PMT2 haploid mutants grow slightly slower than the wild-type, the enzyme is required but not essential for normal vegetative growth of the cells
additional information
P33775, P42934, P52867, Q06644
construction of all single, double and triple mutants of the genes PMT1-4 by gene disruption and crosses, characterization concerning growth, morphology, and their sensitivity to killer toxin K1, sorbitol dependence, caffeine and calcofluor white, overview; construction of all single, double and triple mutants of the genes PMT1-4 by gene disruption and crosses, characterization concerning growth, morphology, and their sensitivity to killer toxin K1, sorbitol dependence, caffeine and calcofluor white, overview; construction of all single, double and triple mutants of the genes PMT1-4 by gene disruption and crosses, characterization concerning growth, morphology, and their sensitivity to killer toxin K1, sorbitol dependence, caffeine and calcofluor white, overview; construction of all single, double and triple mutants of the genes PMT1-4 by gene disruption and crosses, characterization concerning growth, morphology, and their sensitivity to killer toxin K1, sorbitol dependence, caffeine and calcofluor white, overview
additional information
-
construction of defective mutants of PMT1-4,6, determination of substrate specificities
additional information
-
construction of diverse deletion mutants of PMT1, effect on activity and complex formation with PMT2, overview
W253A
-
site-directed mutagenesis, exchange of conserved residue in the central loop, slightly reduced activity
additional information
Q4P140, Q4P339, Q4P380
complementation studies with Schizosaccharomyces pombe deletion mutants show that pmt1 is a functional homolog; complementation studies with Schizosaccharomyces pombe deletion mutants show that pmt4 is a functional homolog; pmt2 deletion mutants are not viable; pmt4 and pmt1 and double deletion mutants are viable with normal growth rates and mating, normal disease symptoms are developed in infected Zea mays; pmt4 and pmt1 and double deletion mutants are viable with normal growth rates and mating, normal disease symptoms are developed in infected Zea mays; the single deletion mutant of pmt1 is viable with normal growth rates and mating, causes disease development in Zea may comparable to wild-type, no increased sensitivity to antifungal substances such as congo red, chlorpromazine, calcofluor white, and caffein or to thermal stress (34 and 36C), oxidative stress (H2O2), osmotic stress (SDS and sorbitol), or salt-based stress (NaCl, CaCl2); the single deletion mutant of pmt4 is viable with normal growth rates and mating, causes no disease symptoms in Zea mays, not even in plants infected via the stigma, no increased sensitivity to antifungal substances such as congo red, chlorpromazine, calcofluor white, and caffein or to thermal stress (34 and 36C), to oxidative stress (H2O2), to osmotic stress by sorbitol but to SDS, or to salt-based stress (NaCl, CaCl2), no changed activity of secreted hydrolytic enzymes (cellulase, pectinase, amylase activity), normal filament formation but lower appressorium formation and aberrant appressorium formation, hyphae are built close to the plant surface but do not intrude the epidermal cell layer, inhibition of the defensive plant reactive oxygen species formation does not restore virulence
additional information
-
deletion mutants show reduced virulence
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
medicine
-
protein O-mannosyltransferase isoforms regulate biofilm formation in Candida albicans. Inhibition may prevent surface anchoring and biofilm-dependent resistance of fungal pathogens
medicine
-, Q59X23, Q5ADM9
Pmt proteins may be suitable targets for future novel classes of antifungal agents; Pmt proteins may be suitable targets for future novel classes of antifungal agents; Pmt proteins may be suitable targets for future novel classes of antifungal agents; Pmt proteins may be suitable targets for future novel classes of antifungal agents; Pmt proteins may be suitable targets for future novel classes of antifungal agents
medicine
-
using Drosophila as model for investigating the mechanisms of human congenital muscular dystrophies (dystroglycanopathies) resulting from the abnormal glycosylation of alpha-dystroglycan
diagnostics
Q9Y6A1
analysis of fibroblasts to elucidate the phenotypes of POMT1 mutations
medicine
-
POMT1 mutations in patients with congenital muscular dystrophy (Italian population); POMT2 mutations in patients with congenital muscular dystrophy (Italian population)
agriculture
Q4P140, Q4P339, Q4P380
Ustilago maydis enzyme homologs are not found in plants and may be a new target for fungal control strategies, research into mechanisms of fungal plant penetration; Ustilago maydis enzyme homologs are not found in plants and may be a new target for fungal control strategies, research into mechanisms of fungal plant penetration; Ustilago maydis enzyme homologs are not found in plants and may be a new target for fungal control strategies, research into mechanisms of fungal plant penetration