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dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
dolichyl phosphate D-mannose + Tyr-Ala-Thr-Ala-Val
dolichyl phosphate + O-D-mannosyl-Tyr-Ala-Thr-Ala-Val
wild-type and mutants
-
?
dolichyl D-mannosyl phosphate + YATAVK-Btn
dolichyl phosphate + O-D-mannosyl-YATAVK-Btn
photocross-linking reaction based on the peptide YATAVK-Btn that serves as in vitro mannosyl acceptor substrate of Pmt1p/Pmt2p and is O -mannosylated to a similar extent as the known acceptor peptide AcNH-YATAV-CONH2
-
-
?
dolichyl phosphate D-mannose + Ac-Tyr-Ala-Thr-Ala-Val-NH2
dolichyl phosphate + O-D-mannosyl-Ac-Tyr-Ala-Thr-Ala-Val-NH2
dolichyl phosphate D-mannose + Ac-Tyr-Asn-Pro-Thr-Ser-Val-NH2
dolichyl phosphate + O-D-mannosyl-Ac-Tyr-Asn-Pro-Thr-Ser-Val-NH2
dolichyl phosphate D-mannose + AcSSSSSNH2
dolichyl phosphate + O-D-mannosyl-AcSSSSSNH2
dolichyl phosphate D-mannose + Asn-Ala-Thr-Val-dinitrophenyl
dolichyl phosphate + O-D-mannosyl-Asn-Ala-Thr-Val-dinitrophenyl
-
-
-
?
dolichyl phosphate D-mannose + biotin-Tyr-Ala-Thr-Ala-Val-NH2
dolichyl phosphate + O-D-mannosyl-N-biotinyl-Tyr-Ala-Thr-Ala-Val-NH2
-
-
-
?
dolichyl phosphate D-mannose + Gas1p
dolichyl phosphate + O-D-mannosyl-Gas1p
-
-
-
-
?
dolichyl phosphate D-mannose + Lys-Pro-Ser-Gly-Tyr
dolichyl phosphate + O-D-mannosyl-Lys-Pro-Ser-Gly-Tyr
-
-
-
?
dolichyl phosphate D-mannose + Lys-Pro-Thr-Gly-Tyr
dolichyl phosphate + O-D-mannosyl-Lys-Pro-Thr-Gly-Tyr
-
-
-
?
dolichyl phosphate D-mannose + Lys-Pro-Thr-Pro-Tyr
dolichyl phosphate + O-D-mannosyl-Lys-Pro-Thr-Pro-Tyr
-
-
-
?
dolichyl phosphate D-mannose + Pro-Thr-Val
dolichyl phosphate + O-D-mannosyl-Pro-Thr-Val
-
-
-
?
dolichyl phosphate D-mannose + Pro-Tyr-Thr-Val
dolichyl phosphate + O-D-mannosyl-Pro-Tyr-Thr-Val
-
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
dolichyl phosphate D-mannose + protein Aga2
dolichyl phosphate + O-D-mannosylprotein Aga2
dolichyl phosphate D-mannose + protein Bar1
dolichyl phosphate + O-D-mannosylprotein Bar1
dolichyl phosphate D-mannose + protein chitinase 1
dolichyl phosphate + O-D-mannosylprotein chitinase 1
dolichyl phosphate D-mannose + protein Ggp1/Gas1
dolichyl phosphate + O-D-mannosylprotein Ggp1/Gas1
dolichyl phosphate D-mannose + protein Kex2
dolichyl phosphate + O-D-mannosylprotein Kex2
dolichyl phosphate D-mannose + protein Kre9
dolichyl phosphate + O-D-mannosylprotein Kre9
dolichyl phosphate D-mannose + protein Pir2/hsp150
dolichyl phosphate + O-D-mannosylprotein Pir2/hsp150
dolichyl phosphate D-mannose + RSPSPSTQ
dolichyl phosphate + O-D-mannosyl-RSPSPSTQ
-
-
-
?
dolichyl phosphate D-mannose + Tyr-Ala-Thr-Ala-Val
dolichyl phosphate + O-D-mannosyl-Tyr-Ala-Thr-Ala-Val
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
-
-
-
?
dolichyl phosphate D-mannose + Tyr-Asn-Pro-Thr-Ser-Val
dolichyl phosphate + O-D-mannosyl-Tyr-Asn-Pro-Thr-Ser-Val
dolichyl phosphate D-mannose + Tyr-Asn-Pro-Thr-Ser-Val-NH2
dolichyl phosphate + O-alpha-D-mannosyl-Tyr-Asn-Pro-Thr-Ser-Val-NH2
-
-
-
?
additional information
?
-
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
the enzyme transfers mannosyl residues to the hydroxyl of serine or threonine residues
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
acceptor substrates: secretory proteins
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
acceptor substrates: secretory proteins
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
production of cell-wall mannoproteins
-
-
?
dolichyl phosphate D-mannose + Ac-Tyr-Ala-Thr-Ala-Val-NH2
dolichyl phosphate + O-D-mannosyl-Ac-Tyr-Ala-Thr-Ala-Val-NH2
-
recombinant yeast overproducing PMT1 and PMT2
-
ir
dolichyl phosphate D-mannose + Ac-Tyr-Ala-Thr-Ala-Val-NH2
dolichyl phosphate + O-D-mannosyl-Ac-Tyr-Ala-Thr-Ala-Val-NH2
-
PMT1
-
?
dolichyl phosphate D-mannose + Ac-Tyr-Ala-Thr-Ala-Val-NH2
dolichyl phosphate + O-D-mannosyl-Ac-Tyr-Ala-Thr-Ala-Val-NH2
-
PMT1 transfers preferably to the threonine and valine residues, the additional enzyme form prefers the serine residue, both depending on the sequence of the acceptor substrate peptide
-
?
dolichyl phosphate D-mannose + Ac-Tyr-Asn-Pro-Thr-Ser-Val-NH2
dolichyl phosphate + O-D-mannosyl-Ac-Tyr-Asn-Pro-Thr-Ser-Val-NH2
-
-
?
dolichyl phosphate D-mannose + Ac-Tyr-Asn-Pro-Thr-Ser-Val-NH2
dolichyl phosphate + O-D-mannosyl-Ac-Tyr-Asn-Pro-Thr-Ser-Val-NH2
-
-
-
ir
dolichyl phosphate D-mannose + AcSSSSSNH2
dolichyl phosphate + O-D-mannosyl-AcSSSSSNH2
-
-
-
ir
dolichyl phosphate D-mannose + AcSSSSSNH2
dolichyl phosphate + O-D-mannosyl-AcSSSSSNH2
-
PMT1-3, PMT5, PMT6, not PMT4
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
-
-
ir
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
acceptor substrate: human-granulocyte-macrophage colony-stimulating-factor-derived peptide(4-11)
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
the enzyme transfers mannosyl residues to the hydroxyl of serine or threonine residues
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
the enzyme transfers mannosyl residues to the hydroxyl of serine or threonine residues
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
the enzyme transfers mannosyl residues to the hydroxyl of serine or threonine residues
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
the enzyme transfers mannosyl residues to the hydroxyl of serine or threonine residues
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
the enzyme transfers mannosyl residues to the hydroxyl of serine or threonine residues
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
the enzyme transfers mannosyl residues to the hydroxyl of serine or threonine residues
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
the enzyme transfers mannosyl residues to the hydroxyl of serine or threonine residues
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
the enzyme transfers mannosyl residues to the hydroxyl of serine or threonine residues
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
the enzyme transfers mannosyl residues to the hydroxyl of serine or threonine residues
-
ir
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
the enzyme transfers mannosyl residues to the hydroxyl of serine or threonine residues
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
preferred chain lengthin decreasing order: C100, C80, C55, C35
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
preferred chain lengthin decreasing order: C100, C80, C55, C35
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
acceptor substrate specificity study
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
strictly stereospecific for the anomeric configuration of phosphoryl-linkage of the donor substrate, a saturated alpha-isoprene unit in the dolichyl moiety is required
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
acidic amino acids strongly inhibit acceptor activity, as do glycine and proline residues as amino-terminal and carboxy-terminal neighbours
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
acceptor substrate: HCl-treated cell wall mannoprotein from Saccharomyces cerevisiae
-
ir
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
acceptor substrate specificities of PMT1-4,6
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
acceptor substrates: secretory proteins
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
acceptor substrates: secretory proteins
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
production of cell-wall mannoproteins
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
production of cell-wall mannoproteins
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
production of cell-wall mannoproteins
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
production of cell-wall mannoproteins
-
-
?
dolichyl phosphate D-mannose + protein Aga2
dolichyl phosphate + O-D-mannosylprotein Aga2
-
i.e. small-agglutinin
-
?
dolichyl phosphate D-mannose + protein Aga2
dolichyl phosphate + O-D-mannosylprotein Aga2
-
activity is not affected by disruption mutations of PMT1-4
-
?
dolichyl phosphate D-mannose + protein Aga2
dolichyl phosphate + O-D-mannosylprotein Aga2
-
protein is located at the cell surface
-
-
?
dolichyl phosphate D-mannose + protein Bar1
dolichyl phosphate + O-D-mannosylprotein Bar1
-
PMT1 and PMT2, not PMT3 and PMT4
-
?
dolichyl phosphate D-mannose + protein Bar1
dolichyl phosphate + O-D-mannosylprotein Bar1
-
protein is located in the medium
-
-
?
dolichyl phosphate D-mannose + protein chitinase 1
dolichyl phosphate + O-D-mannosylprotein chitinase 1
-
PMT1
-
?
dolichyl phosphate D-mannose + protein chitinase 1
dolichyl phosphate + O-D-mannosylprotein chitinase 1
-
PMT1, PMT4, PMT6 and especially PMT2, not PMT3
-
?
dolichyl phosphate D-mannose + protein chitinase 1
dolichyl phosphate + O-D-mannosylprotein chitinase 1
-
protein is located in the cell wall and medium
-
-
?
dolichyl phosphate D-mannose + protein Ggp1/Gas1
dolichyl phosphate + O-D-mannosylprotein Ggp1/Gas1
-
PMT4 and PMT6, not PMT1-3
-
?
dolichyl phosphate D-mannose + protein Ggp1/Gas1
dolichyl phosphate + O-D-mannosylprotein Ggp1/Gas1
-
protein is located at the cell surface
-
-
?
dolichyl phosphate D-mannose + protein Kex2
dolichyl phosphate + O-D-mannosylprotein Kex2
-
PMT4, not PMT1-3
-
?
dolichyl phosphate D-mannose + protein Kex2
dolichyl phosphate + O-D-mannosylprotein Kex2
-
protein is located in the Golgi apparatus
-
-
?
dolichyl phosphate D-mannose + protein Kre9
dolichyl phosphate + O-D-mannosylprotein Kre9
-
mainly PMT1 and PMT2, not PMT3 and PMT4
-
?
dolichyl phosphate D-mannose + protein Kre9
dolichyl phosphate + O-D-mannosylprotein Kre9
-
protein is located in the Golgi apparatus
-
-
?
dolichyl phosphate D-mannose + protein Pir2/hsp150
dolichyl phosphate + O-D-mannosylprotein Pir2/hsp150
-
PMT1
-
?
dolichyl phosphate D-mannose + protein Pir2/hsp150
dolichyl phosphate + O-D-mannosylprotein Pir2/hsp150
-
PMT1, PMT2, and to some extent PMT4, not PMT3
-
?
dolichyl phosphate D-mannose + protein Pir2/hsp150
dolichyl phosphate + O-D-mannosylprotein Pir2/hsp150
-
protein is located in the medium
-
-
?
dolichyl phosphate D-mannose + Tyr-Asn-Pro-Thr-Ser-Val
dolichyl phosphate + O-D-mannosyl-Tyr-Asn-Pro-Thr-Ser-Val
-
-
-
?
dolichyl phosphate D-mannose + Tyr-Asn-Pro-Thr-Ser-Val
dolichyl phosphate + O-D-mannosyl-Tyr-Asn-Pro-Thr-Ser-Val
-
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
-
-
?
additional information
?
-
-
-
-
?
additional information
?
-
-
PMT3: no clearly determined dolichyl-phosphate-mannose-protein mannosyltransferase activity
-
-
?
additional information
?
-
-
PMT4 and PMT6 probably function as an active dimer
-
-
?
additional information
?
-
-
PMT1 and PMT2 function as a complex
-
-
?
additional information
?
-
-
PMT1 and PMT2 function as a complex
-
-
?
additional information
?
-
-
PMT3 behaves as a dolichyl-phosphate-mannose-glycolipid alpha-mannosyltransferase, EC 2.4.1.130
-
-
?
additional information
?
-
PMT3 behaves as a dolichyl-phosphate-mannose-glycolipid alpha-mannosyltransferase, EC 2.4.1.130
-
-
?
additional information
?
-
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
dolichyl phosphate D-mannose + protein Aga2
dolichyl phosphate + O-D-mannosylprotein Aga2
dolichyl phosphate D-mannose + protein Bar1
dolichyl phosphate + O-D-mannosylprotein Bar1
dolichyl phosphate D-mannose + protein chitinase 1
dolichyl phosphate + O-D-mannosylprotein chitinase 1
dolichyl phosphate D-mannose + protein Ggp1/Gas1
dolichyl phosphate + O-D-mannosylprotein Ggp1/Gas1
dolichyl phosphate D-mannose + protein Kex2
dolichyl phosphate + O-D-mannosylprotein Kex2
dolichyl phosphate D-mannose + protein Kre9
dolichyl phosphate + O-D-mannosylprotein Kre9
dolichyl phosphate D-mannose + protein Pir2/hsp150
dolichyl phosphate + O-D-mannosylprotein Pir2/hsp150
additional information
?
-
-
defective mutants are used to investigate the substrate specificities of PMT1-4,6 in vivo
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
acceptor substrates: secretory proteins
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
production of cell-wall mannoproteins
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
-
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
-
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
acceptor substrate specificities of PMT1-4,6
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
acceptor substrates: secretory proteins
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
production of cell-wall mannoproteins
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
production of cell-wall mannoproteins
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
production of cell-wall mannoproteins
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
production of cell-wall mannoproteins
-
-
?
dolichyl phosphate D-mannose + protein Aga2
dolichyl phosphate + O-D-mannosylprotein Aga2
-
i.e. small-agglutinin
-
-
?
dolichyl phosphate D-mannose + protein Aga2
dolichyl phosphate + O-D-mannosylprotein Aga2
-
activity is not affected by disruption mutations of PMT1-4
-
-
?
dolichyl phosphate D-mannose + protein Aga2
dolichyl phosphate + O-D-mannosylprotein Aga2
-
protein is located at the cell surface
-
-
?
dolichyl phosphate D-mannose + protein Bar1
dolichyl phosphate + O-D-mannosylprotein Bar1
-
PMT1 and PMT2, not PMT3 and PMT4
-
-
?
dolichyl phosphate D-mannose + protein Bar1
dolichyl phosphate + O-D-mannosylprotein Bar1
-
protein is located in the medium
-
-
?
dolichyl phosphate D-mannose + protein chitinase 1
dolichyl phosphate + O-D-mannosylprotein chitinase 1
-
PMT1
-
-
?
dolichyl phosphate D-mannose + protein chitinase 1
dolichyl phosphate + O-D-mannosylprotein chitinase 1
-
PMT1, PMT4, PMT6 and especially PMT2, not PMT3
-
-
?
dolichyl phosphate D-mannose + protein chitinase 1
dolichyl phosphate + O-D-mannosylprotein chitinase 1
-
protein is located in the cell wall and medium
-
-
?
dolichyl phosphate D-mannose + protein Ggp1/Gas1
dolichyl phosphate + O-D-mannosylprotein Ggp1/Gas1
-
PMT4 and PMT6, not PMT1-3
-
-
?
dolichyl phosphate D-mannose + protein Ggp1/Gas1
dolichyl phosphate + O-D-mannosylprotein Ggp1/Gas1
-
protein is located at the cell surface
-
-
?
dolichyl phosphate D-mannose + protein Kex2
dolichyl phosphate + O-D-mannosylprotein Kex2
-
PMT4, not PMT1-3
-
-
?
dolichyl phosphate D-mannose + protein Kex2
dolichyl phosphate + O-D-mannosylprotein Kex2
-
protein is located in the Golgi apparatus
-
-
?
dolichyl phosphate D-mannose + protein Kre9
dolichyl phosphate + O-D-mannosylprotein Kre9
-
mainly PMT1 and PMT2, not PMT3 and PMT4
-
-
?
dolichyl phosphate D-mannose + protein Kre9
dolichyl phosphate + O-D-mannosylprotein Kre9
-
protein is located in the Golgi apparatus
-
-
?
dolichyl phosphate D-mannose + protein Pir2/hsp150
dolichyl phosphate + O-D-mannosylprotein Pir2/hsp150
-
PMT1
-
-
?
dolichyl phosphate D-mannose + protein Pir2/hsp150
dolichyl phosphate + O-D-mannosylprotein Pir2/hsp150
-
PMT1, PMT2, and to some extent PMT4, not PMT3
-
-
?
dolichyl phosphate D-mannose + protein Pir2/hsp150
dolichyl phosphate + O-D-mannosylprotein Pir2/hsp150
-
protein is located in the medium
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
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construction of diverse deletion mutants of PMT1, effect on activity and complex formation with PMT2, overview
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
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
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
additional information
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 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 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 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 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 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 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
-
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
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PMT2 disruption mutant shows reduced in vitro and in vivo activity
additional information
PMT2 disruption mutant shows reduced in vitro and in vivo activity
additional information
-
PMT1 and PMT2 double disruption mutant shows severe growth defect but retain residual activity due to an additional enzyme
additional information
PMT1 and PMT2 double disruption mutant shows severe growth defect but retain residual activity due to an additional enzyme
additional information
-
PMT3 and 4 gene disruption does not alter enzyme activity
additional information
PMT3 and 4 gene disruption does not alter enzyme activity
additional information
PMT3 and 4 gene disruption does not alter enzyme activity
additional information
-
construction of defective mutants of PMT1-4,6, determination of substrate specificities
additional information
-
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
PMT2 haploid mutants grow slightly slower than the wild-type, the enzyme is required but not essential for normal vegetative growth of the cells
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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
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Saccharomyces cerevisiae
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PMT3 and PMT4, two new members of the protein-O-mannosyltransferase gene family of Saccharomyces cerevisiae
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Saccharomyces cerevisiae, Saccharomyces cerevisiae (P46971), Saccharomyces cerevisiae (P47190)
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Saccharomyces cerevisiae
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Saccharomyces cerevisiae
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A new Dol-P-Man:protein O-D-mannosyltransferase activity from Saccharomyces cerevisiae
Glycobiology
5
77-82
1995
Saccharomyces cerevisiae
brenda
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
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1995
Saccharomyces cerevisiae, Saccharomyces cerevisiae (P31382)
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Gentzsch, M.; Tanner, W.
The PMT gene family: protein O-glycosylation in Saccharomyces cerevisiae is vital
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15
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Saccharomyces cerevisiae (P31382), Saccharomyces cerevisiae (P33775), Saccharomyces cerevisiae (P42934), Saccharomyces cerevisiae (P46971), Saccharomyces cerevisiae (P47190), Saccharomyces cerevisiae (P52867), Saccharomyces cerevisiae (Q06644)
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Gentzsch, M.; Tanner, W.
Protein-O-glycosylation in yeast: protein-specific mannosyltransferases
Glycobiology
7
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1997
Saccharomyces cerevisiae
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Girrbach, V.; Zeller, T.; Priesmeier, M.; Strahl-Bolsinger, S.
Structure-function analysis of the dolichyl phosphate-mannose:protein O-mannosyltransferase ScPmt1p
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275
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2000
Saccharomyces cerevisiae
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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
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2002
Saccharomyces cerevisiae, Saccharomyces cerevisiae BY4743
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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)
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Goder, V.; Melero, A.
Protein O-mannosyltransferases participate in ER protein quality control
J. Cell Sci.
124
144-153
2011
Saccharomyces cerevisiae
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Loibl, M.; Strahl, S.
Photoaffinity labeling of protein O-mannosyltransferases of the PMT1/PMT2 subfamily
Methods Mol. Biol.
1022
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2013
Saccharomyces cerevisiae (P33775), Saccharomyces cerevisiae
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