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

New: Word Map on EC 2.4.1.109
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Mark a special word or phrase in this record:
Search Reference ID:
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


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

EC NUMBER
COMMENTARY hide
2.4.1.109
-
RECOMMENDED NAME
GeneOntology No.
dolichyl-phosphate-mannose-protein mannosyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
dolichyl D-mannosyl phosphate + protein = dolichyl phosphate + O-D-mannosylprotein
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexosyl group transfer
-
-
-
-
PATHWAY
BRENDA Link
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.
CAS REGISTRY NUMBER
COMMENTARY hide
74315-99-4
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
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
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain BY4743
-
-
Manually annotated by BRENDA team
-
Uniprot
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
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-Asn-Pro-Thr-Ser-Val-NH2
dolichyl phosphate + O-D-mannosyl-Ac-Tyr-Asn-Pro-Thr-Ser-Val-NH2
show the reaction diagram
dolichyl phosphate D-mannose + AcSSSSSNH2
dolichyl phosphate + O-D-mannosyl-AcSSSSSNH2
show the reaction diagram
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
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-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
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-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-[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 + human ribonuclease 2
dolichyl phosphate + human ribonuclease 2-D-mannose
show the reaction diagram
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 Aga2
dolichyl phosphate + O-D-mannosylprotein Aga2
show the reaction diagram
dolichyl phosphate D-mannose + protein AN5660
dolichyl phosphate + O-D-mannosylprotein
show the reaction diagram
dolichyl phosphate D-mannose + protein Bar1
dolichyl phosphate + O-D-mannosylprotein Bar1
show the reaction diagram
dolichyl phosphate D-mannose + protein chitinase 1
dolichyl phosphate + O-D-mannosylprotein chitinase 1
show the reaction diagram
dolichyl phosphate D-mannose + protein Ggp1/Gas1
dolichyl phosphate + O-D-mannosylprotein Ggp1/Gas1
show the reaction diagram
dolichyl phosphate D-mannose + protein Kex2
dolichyl phosphate + O-D-mannosylprotein Kex2
show the reaction diagram
dolichyl phosphate D-mannose + protein Kre9
dolichyl phosphate + O-D-mannosylprotein Kre9
show the reaction diagram
dolichyl phosphate D-mannose + protein Pir2/hsp150
dolichyl phosphate + O-D-mannosylprotein Pir2/hsp150
show the reaction diagram
dolichyl phosphate D-mannose + ribonuclease 2
dolichyl phosphate + ribonuclease 2-D-mannose
show the reaction diagram
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-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-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
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
dolichyl 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 Aga2
dolichyl phosphate + O-D-mannosylprotein Aga2
show the reaction diagram
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
dolichyl phosphate D-mannose + protein chitinase 1
dolichyl phosphate + O-D-mannosylprotein chitinase 1
show the reaction diagram
dolichyl phosphate D-mannose + protein Ggp1/Gas1
dolichyl phosphate + O-D-mannosylprotein Ggp1/Gas1
show the reaction diagram
dolichyl phosphate D-mannose + protein Kex2
dolichyl phosphate + O-D-mannosylprotein Kex2
show the reaction diagram
dolichyl phosphate D-mannose + protein Kre9
dolichyl phosphate + O-D-mannosylprotein Kre9
show the reaction diagram
dolichyl phosphate D-mannose + protein Pir2/hsp150
dolichyl phosphate + O-D-mannosylprotein Pir2/hsp150
show the reaction diagram
dolichyl phosphate D-mannose + ribonuclease 2
dolichyl phosphate + ribonuclease 2-D-mannose
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mn2+
-
Mg2+ or Mn2+ stimulates
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Chymotrypsin
-
inactivation
-
CuSO4
-
10 mM, complete inhibition
glycerol
phosphatidylinositol
-
-
additional information
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
deoxycholate
-
0.025%, stimulates slightly
EDTA
-
up to 3fold stimulation
phosphatidylcholine
-
stimulates
phosphatidylglycerol
-
-
phosphatidylinositol
-
-
additional information
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
6.7
Ac-Ala-Thr-Ala-NH2
-
-
0.25 - 15
Ac-Tyr-Ala-Thr-Ala-Val-NH2
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
-
-
0.4
dolichyl phosphate D-mannose
-
-
10 - 20
RSPSPSTQ
0.63 - 9.7
synthetic peptide based on a mucin-like domain in alpha-dystroglycan
2.2
Tyr-Ala-Thr-Ala-Val
-
-
1 - 3.3
Tyr-Asn-Pro-Thr-Ser-Val
2.5
Tyr-Leu-Thr-Ala-Val
-
-
7.3
Tyr-Pro-Thr-Ala-Val
-
-
additional information
additional information
-
Km value depends on chain length and alpha-saturation of the acceptor substrate
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0000012
-
substrate YNPTSV
0.0000677
-
partially purified enzyme
0.00057
-
partially purified enzyme
0.0035
-
partially purified enzyme
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.2
-
assay at
7.5 - 8
-
the best buffers are bicine pH 7.7, tricine pH 8.0 and HEPES pH 7.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
-
additional enzyme form
25
-
assay at
37
-
assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
28 - 37
-
in vivo
additional information
-
40% remaining activity at 0C
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
-
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
-
human embryonic kidney
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 expression
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
71000
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
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
Walker-Warburg syndrome p.del77-93 mutant enzyme is not detectable, Western blot analysis, SDS-PAGE with antibody staining
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
heterodimer
-
AnpmtB with AnpmtA, 2 * ?; AnpmtB with AnpmtA, but AnPmtB disruption mutant shows different phenotype than AnpmtA disruptant, independent function
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.9
-
inactivation below pH 4.9
638334
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
26
-
22 h, stable
37
-
60 min, stable
95
-
inactivation
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
stable in solution with deoxycholate and CHAPS
-
STORAGE STABILITY
ORGANISM
UNIPROT
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
LITERATURE
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
gel purification of disruption mutants
-
gel purification of disruption mutants; gel purification of disruption mutants; gel purification of disruption mutants
glutathione Sepharose column chromatography
-
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
-
IgG-coupled magnetic bead chromatography
-
immunoaffinity chromatography, co-purification of PMT1 and PMT2 as a complex, no immuno-cross reactivity
-
partial
partial; solubilization with 0.5% deoxycholate and 1.2% CHAPS
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
; 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
-
expressed in Escherichia coli OrigamiTM (DE 3) cells
-
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
-
expression in Saccharomyces cerevisiae; expression in Saccharomyces cerevisiae; expression in Saccharomyces cerevisiae
-
expression of Pmt4 in a Saccharomyces cerevisiae pmt1pmt4 mutant strain functionally complements the deficient Pmt activity
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
PCR-amplification of blood derived enzyme gene
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
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
PCR-amplification, introduction of replacement cassettes to disrupt genes
-
EXPRESSION
ORGANISM
UNIPROT
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
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
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
L171A
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
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
L408A/H411A
-
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
W253A
-
site-directed mutagenesis, exchange of conserved residue in the central loop, slightly reduced activity
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
diagnostics
analysis of fibroblasts to elucidate the phenotypes of POMT1 mutations
medicine
Show AA Sequence (480 entries)
Please use the Sequence Search for a certain query.