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Information on EC 2.4.1.109 - dolichyl-phosphate-mannose-protein mannosyltransferase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P52867

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EC Tree
IUBMB Comments
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.
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This record set is specific for:
Saccharomyces cerevisiae
UNIPROT: P52867
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Word Map
The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
pomt1, pomt2, protein o-mannosyltransferase, pmt1p, o-mannosyltransferase, protein o-mannosyltransferase 1, pmt2p, pmt1p-pmt2p, pmt4p, aapmta, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dolichol phosphomannose-protein mannosyltransferase
-
-
-
-
dolichyl phosphate-mannose:protein O-mannosyltransferase
-
dolichyl-phosphate-mannose-protein mannosyltransferase
-
-
mannosyltransferase, dolichol phosphomannose-protein
-
-
-
-
Pmt1p
protein mannosyltransferase
-
-
protein O-D-mannosyltransferase
-
-
-
-
protein O-mannosyltransferase
-
-
additional information
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
dolichyl beta-D-mannosyl phosphate + L-threonyl-[protein] = dolichyl phosphate + 3-O-(alpha-D-mannosyl)-L-threonyl-[protein]
show the reaction diagram
structure-function analysis
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexosyl group transfer
-
-
-
-
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
-
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 + protein
dolichyl phosphate + O-D-mannosylprotein
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
wild-type and mutants
-
?
dolichyl D-mannosyl phosphate + YATAVK-Btn
dolichyl phosphate + O-D-mannosyl-YATAVK-Btn
show the reaction diagram
photocross-linking reaction based on the peptide YATAVK-Btn that serves as in vitro mannosyl acceptor substrate of Pmt1p/Pmt2p and is O -mannosylated to a similar extent as the known acceptor peptide AcNH-YATAV-CONH2
-
-
?
dolichyl phosphate D-mannose + Ac-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 + 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 + Gas1p
dolichyl phosphate + O-D-mannosyl-Gas1p
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 + 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 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 + 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
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-NH2
dolichyl phosphate + O-alpha-D-mannosyl-Tyr-Asn-Pro-Thr-Ser-Val-NH2
show the reaction diagram
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL 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 + 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 Aga2
dolichyl phosphate + O-D-mannosylprotein Aga2
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
additional information
?
-
-
defective mutants are used to investigate the substrate specificities of PMT1-4,6 in vivo
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mn2+
-
Mg2+ or Mn2+ stimulates
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
CuSO4
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10 mM, complete inhibition
glycerol
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
deoxycholate
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0.025%, stimulates slightly
additional information
-
not affected by Triton X-100 up to 0.2%
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2 - 15
Ac-Tyr-Ala-Thr-Ala-Val-NH2
0.4
dolichyl phosphate D-mannose
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-
10 - 20
RSPSPSTQ
1 - 3.3
Tyr-Asn-Pro-Thr-Ser-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
0.0000677
-
partially purified enzyme
0.00057
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partially purified enzyme
0.0035
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partially purified enzyme
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
-
additional enzyme form
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
40% remaining activity at 0°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
PMT family members are conserved throughout the fungal and animal kingdoms. They are further subdivided into the PMT1, PMT2, and PMT4 subfamilies, which include transferases closely related to Saccharomyces cerevisiae Pmt1p, Pmt2p, and Pmt4p, respectively. In fungi, at least one member of each subfamily is present, whereas in animals only PMT2 and PMT4 subfamily members are conserved. In Saccharomyces, Pmt1p, Pmt2p, and Pmt4p account for the major transferase activities although at least six PMTs (Pmt1p-Pmt6p) are present
physiological function
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
78000
-
x * 78000, PMT2, SDS-PAGE
92000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.9
-
inactivation below pH 4.9
638334
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
stable in solution with deoxycholate and CHAPS
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, partially purified enzyme, indefinitely stable
-
23°C, partially purified enzyme, 2% glycerol, at least 12 h stable
-
4-23°C, partially purified enzyme, stable for at least 1 week
-
4°C, solubilized with 0.5% Triton X-100, loss of 80% activity within 5 days
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
IgG-coupled magnetic bead chromatography
-
immunoaffinity chromatography, co-purification of PMT1 and PMT2 as a complex, no immuno-cross reactivity
-
native enzyme partially
solubilization with 0.5% deoxycholate and 1.2% CHAPS
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
chromosome mapping of PMT1
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
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DNA sequence determination
DNA sequence determination, chromosome mapping
recombinant expression of HA-tagged isozyme Pmt1p. In Saccharomyces cerevisiae, C-terminal fusions with HA-, FLAG-, or GFP-epitopes do not affect PMTs mannosyltransferase activity
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Babczinski, P.; Haselbeck, A.; Tanner, W.
Yeast mannosyl transferases requiring dolichyl phosphate and dolichyl phosphate mannose as substrate. Partial purification and characterization of the solubilized enzyme
Eur. J. Biochem.
105
509-515
1980
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Palamarczyk, G.; Lehle, L.; Mankowski, T.; Chojnacki, T.; Tanner, W.
Specificity of solubilized yeast glycosyl transferases for polyprenyl derivatives
Eur. J. Biochem.
105
517-523
1980
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Immervoll, T.; Gentzsch, M.; Tanner, W.
PMT3 and PMT4, two new members of the protein-O-mannosyltransferase gene family of Saccharomyces cerevisiae
Yeast
11
1345-1351
1995
Saccharomyces cerevisiae, Saccharomyces cerevisiae (P46971), Saccharomyces cerevisiae (P47190)
Manually annotated by BRENDA team
Strahl-Bolsinger, S.; Tanner, W.
Protein O-glycosylation in Saccharomyces cerevisiae. Purification and characterization of the dolichyl-phosphate-D-mannose-protein O-D-mannosyltransferase
Eur. J. Biochem.
196
185-190
1991
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Lorenz, C.; Strahl-Bolsinger, S.; Ernst, J.F.
Specific in vitro O-glycosylation of human granulocyte-macrophage colony-stimulating-factor-derived peptides by O-glycosyltransferases of yeast and rat liver cells
Eur. J. Biochem.
205
1163-1167
1992
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Dotson, S.B.; Rush, J.S.; Ricketts, A.D.; Waechter, C.J.
Mannosylphosphoryldolichol-mediated O-mannosylation of yeast glycoproteins: stereospecificity and recognition of the alpha-isoprene unit by a purified mannosyltransferase
Arch. Biochem. Biophys.
316
773-779
1995
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Gentzsch, M.; Immervoll, T.; Tanner, W.
Protein O-glycosylation in Saccharomyces cerevisiae: the protein O-mannosyltransferases Pmt1p and Pmt2p function as heterodimer
FEBS Lett.
377
128-130
1995
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Gentzsch, M.; Strahl-Bolsinger, S.; Tanner, W.
A new Dol-P-Man:protein O-D-mannosyltransferase activity from Saccharomyces cerevisiae
Glycobiology
5
77-82
1995
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Lussier, M.; Gentzsch, M.; Sdicu, A.M.; Bussey, H.; Tanner, W.
Protein O-glycosylation in yeast. The PMT2 gene specifies a second protein O-mannosyltransferase that functions in addition to the PMT-1 encoded activity
J. Biol. Chem.
270
2770-2775
1995
Saccharomyces cerevisiae, Saccharomyces cerevisiae (P31382)
Manually annotated by BRENDA team
Gentzsch, M.; Tanner, W.
The PMT gene family: protein O-glycosylation in Saccharomyces cerevisiae is vital
EMBO J.
15
5752-5759
1996
Saccharomyces cerevisiae (P31382), Saccharomyces cerevisiae (P33775), Saccharomyces cerevisiae (P42934), Saccharomyces cerevisiae (P46971), Saccharomyces cerevisiae (P47190), Saccharomyces cerevisiae (P52867), Saccharomyces cerevisiae (Q06644)
Manually annotated by BRENDA team
Gentzsch, M.; Tanner, W.
Protein-O-glycosylation in yeast: protein-specific mannosyltransferases
Glycobiology
7
481-486
1997
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Girrbach, V.; Zeller, T.; Priesmeier, M.; Strahl-Bolsinger, S.
Structure-function analysis of the dolichyl phosphate-mannose:protein O-mannosyltransferase ScPmt1p
J. Biol. Chem.
275
19288-19296
2000
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Hendershot, L.L.; Aeed, P.A.; Kezdy, F.J.; Elhammer, A.P.
An efficient assay for dolichyl phosphate-mannose: protein O-mannosyltransferase
Anal. Biochem.
307
273-279
2002
Saccharomyces cerevisiae, Saccharomyces cerevisiae BY4743
Manually annotated by BRENDA team
Lengeler, K.B.; Tielker, D.; Ernst, J.F.
Protein-O-mannosyltransferases in virulence and development
Cell. Mol. Life Sci.
65
528-544
2008
Candida albicans (O74189), Candida albicans (Q59X23), Candida albicans (Q5ACU3), Candida albicans (Q5ADM9), Candida albicans (Q9UVB5), Cryptococcus neoformans, Mycobacterium tuberculosis, Saccharomyces cerevisiae (P31382), Saccharomyces cerevisiae (P33775), Saccharomyces cerevisiae (P42934), Saccharomyces cerevisiae (P46971), Saccharomyces cerevisiae (P47190), Saccharomyces cerevisiae (P52867), Saccharomyces cerevisiae (Q06644), Schizosaccharomyces pombe (O13898), Schizosaccharomyces pombe (O42933), Schizosaccharomyces pombe (Q9C100)
Manually annotated by BRENDA team
Goder, V.; Melero, A.
Protein O-mannosyltransferases participate in ER protein quality control
J. Cell Sci.
124
144-153
2011
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Loibl, M.; Strahl, S.
Photoaffinity labeling of protein O-mannosyltransferases of the PMT1/PMT2 subfamily
Methods Mol. Biol.
1022
107-117
2013
Saccharomyces cerevisiae (P33775), Saccharomyces cerevisiae
Manually annotated by BRENDA team