BRENDA - Enzyme Database

Structure-function analysis of the dolichyl phosphate-mannose:protein O-mannosyltransferase ScPmt1p

Girrbach, V.; Zeller, T.; Priesmeier, M.; Strahl-Bolsinger, S.; J. Biol. Chem. 275, 19288-19296 (2000)

Data extracted from this reference:

Engineering
EC Number
Amino acid exchange
Commentary
Organism
2.4.1.109
D96A
site-directed mutagenesis, exchange of conserved residue in the central loop, reduced activity
Saccharomyces cerevisiae
2.4.1.109
E78A
site-directed mutagenesis, exchange of conserved residue in the central loop, highly reduced activity
Saccharomyces cerevisiae
2.4.1.109
H346A/H348A
site-directed mutagenesis, exchange of conserved residue in the central loop, reduced activity
Saccharomyces cerevisiae
2.4.1.109
H411A
site-directed mutagenesis, exchange of conserved residue in the central loop, slightly reduced activity
Saccharomyces cerevisiae
2.4.1.109
H472A
site-directed mutagenesis, exchange of conserved residue in the central loop, reduced activity
Saccharomyces cerevisiae
2.4.1.109
K234A
site-directed mutagenesis, exchange of conserved residue in the central loop, slightly reduced activity
Saccharomyces cerevisiae
2.4.1.109
L399A
site-directed mutagenesis, exchange of conserved residue in the central loop, reduced activity
Saccharomyces cerevisiae
2.4.1.109
L408A
site-directed mutagenesis, exchange of conserved residue in the central loop, highly reduced activity
Saccharomyces cerevisiae
2.4.1.109
L408A/H411A
site-directed mutagenesis, exchange of conserved residue in the central loop, highly reduced activity
Saccharomyces cerevisiae
2.4.1.109
additional information
construction of diverse deletion mutants of PMT1, effect on activity and complex formation with PMT2, overview
Saccharomyces cerevisiae
2.4.1.109
N370A
site-directed mutagenesis, exchange of conserved residue in the central loop, slightly reduced activity
Saccharomyces cerevisiae
2.4.1.109
Q359A/Q360A
site-directed mutagenesis, exchange of conserved residue in the central loop, reduced activity
Saccharomyces cerevisiae
2.4.1.109
Q493A/E495A
site-directed mutagenesis, exchange of conserved residue in the central loop, reduced activity
Saccharomyces cerevisiae
2.4.1.109
R138A
site-directed mutagenesis, exchange of conserved residue in the central loop, highly reduced activity
Saccharomyces cerevisiae
2.4.1.109
R398A
site-directed mutagenesis, exchange of conserved residue in the central loop, reduced activity
Saccharomyces cerevisiae
2.4.1.109
R469A
site-directed mutagenesis, exchange of conserved residue in the central loop, slightly reduced activity
Saccharomyces cerevisiae
2.4.1.109
R64 A
site-directed mutagenesis, exchange of conserved residue in the central loop, highly reduced activity
Saccharomyces cerevisiae
2.4.1.109
W253A
site-directed mutagenesis, exchange of conserved residue in the central loop, slightly reduced activity
Saccharomyces cerevisiae
Localization
EC Number
Localization
Commentary
Organism
GeneOntology No.
Textmining
2.4.1.109
endoplasmic reticulum
integral membrane protein
Saccharomyces cerevisiae
5783
-
2.4.1.109
membrane
integral, multiple transmembranal domains
Saccharomyces cerevisiae
16020
-
Natural Substrates/ Products (Substrates)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
2.4.1.109
dolichyl phosphate D-mannose + protein
Saccharomyces cerevisiae
-
dolichyl phosphate + O-D-mannosylprotein
-
-
-
2.4.1.109
dolichyl phosphate D-mannose + protein chitinase 1
Saccharomyces cerevisiae
PMT1
dolichyl phosphate + O-D-mannosylprotein chitinase 1
-
-
-
2.4.1.109
dolichyl phosphate D-mannose + protein Pir2/hsp150
Saccharomyces cerevisiae
PMT1
dolichyl phosphate + O-D-mannosylprotein Pir2/hsp150
-
-
-
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
2.4.1.109
Saccharomyces cerevisiae
-
gene PMT1; gene PMT2
-
Posttranslational Modification
EC Number
Posttranslational Modification
Commentary
Organism
2.4.1.109
glycoprotein
construction of diverse deletion mutants with different numbers of N-glycosylation sites; PMT1: 3 N-glycosylation sites
Saccharomyces cerevisiae
Reaction
EC Number
Reaction
Commentary
Organism
2.4.1.109
dolichyl beta-D-mannosyl phosphate + L-threonyl-[protein] = dolichyl phosphate + 3-O-(alpha-D-mannosyl)-L-threonyl-[protein]
structure-function analysis
Saccharomyces cerevisiae
Specific Activity [micromol/min/mg]
EC Number
Specific Activity Minimum [Ámol/min/mg]
Specific Activity Maximum [Ámol/min/mg]
Commentary
Organism
2.4.1.109
additional information
-
wild-type and deletion mutants
Saccharomyces cerevisiae
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2.4.1.109
dolichyl phosphate D-mannose + Ac-Tyr-Ala-Thr-Ala-Val-NH2
PMT1
638342
Saccharomyces cerevisiae
dolichyl phosphate + O-D-mannosyl-Ac-Tyr-Ala-Thr-Ala-Val-NH2
-
638342
Saccharomyces cerevisiae
?
2.4.1.109
dolichyl phosphate D-mannose + protein
-
638342
Saccharomyces cerevisiae
dolichyl phosphate + O-D-mannosylprotein
-
-
-
-
2.4.1.109
dolichyl phosphate D-mannose + protein
-
638342
Saccharomyces cerevisiae
dolichyl phosphate + O-D-mannosylprotein
-
638342
Saccharomyces cerevisiae
?
2.4.1.109
dolichyl phosphate D-mannose + protein chitinase 1
PMT1
638342
Saccharomyces cerevisiae
dolichyl phosphate + O-D-mannosylprotein chitinase 1
-
-
-
-
2.4.1.109
dolichyl phosphate D-mannose + protein chitinase 1
PMT1
638342
Saccharomyces cerevisiae
dolichyl phosphate + O-D-mannosylprotein chitinase 1
-
638342
Saccharomyces cerevisiae
?
2.4.1.109
dolichyl phosphate D-mannose + protein Pir2/hsp150
PMT1
638342
Saccharomyces cerevisiae
dolichyl phosphate + O-D-mannosylprotein Pir2/hsp150
-
-
-
-
2.4.1.109
dolichyl phosphate D-mannose + protein Pir2/hsp150
PMT1
638342
Saccharomyces cerevisiae
dolichyl phosphate + O-D-mannosylprotein Pir2/hsp150
-
638342
Saccharomyces cerevisiae
?
Subunits
EC Number
Subunits
Commentary
Organism
2.4.1.109
More
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
Saccharomyces cerevisiae
Engineering (protein specific)
EC Number
Amino acid exchange
Commentary
Organism
2.4.1.109
D96A
site-directed mutagenesis, exchange of conserved residue in the central loop, reduced activity
Saccharomyces cerevisiae
2.4.1.109
E78A
site-directed mutagenesis, exchange of conserved residue in the central loop, highly reduced activity
Saccharomyces cerevisiae
2.4.1.109
H346A/H348A
site-directed mutagenesis, exchange of conserved residue in the central loop, reduced activity
Saccharomyces cerevisiae
2.4.1.109
H411A
site-directed mutagenesis, exchange of conserved residue in the central loop, slightly reduced activity
Saccharomyces cerevisiae
2.4.1.109
H472A
site-directed mutagenesis, exchange of conserved residue in the central loop, reduced activity
Saccharomyces cerevisiae
2.4.1.109
K234A
site-directed mutagenesis, exchange of conserved residue in the central loop, slightly reduced activity
Saccharomyces cerevisiae
2.4.1.109
L399A
site-directed mutagenesis, exchange of conserved residue in the central loop, reduced activity
Saccharomyces cerevisiae
2.4.1.109
L408A
site-directed mutagenesis, exchange of conserved residue in the central loop, highly reduced activity
Saccharomyces cerevisiae
2.4.1.109
L408A/H411A
site-directed mutagenesis, exchange of conserved residue in the central loop, highly reduced activity
Saccharomyces cerevisiae
2.4.1.109
additional information
construction of diverse deletion mutants of PMT1, effect on activity and complex formation with PMT2, overview
Saccharomyces cerevisiae
2.4.1.109
N370A
site-directed mutagenesis, exchange of conserved residue in the central loop, slightly reduced activity
Saccharomyces cerevisiae
2.4.1.109
Q359A/Q360A
site-directed mutagenesis, exchange of conserved residue in the central loop, reduced activity
Saccharomyces cerevisiae
2.4.1.109
Q493A/E495A
site-directed mutagenesis, exchange of conserved residue in the central loop, reduced activity
Saccharomyces cerevisiae
2.4.1.109
R138A
site-directed mutagenesis, exchange of conserved residue in the central loop, highly reduced activity
Saccharomyces cerevisiae
2.4.1.109
R398A
site-directed mutagenesis, exchange of conserved residue in the central loop, reduced activity
Saccharomyces cerevisiae
2.4.1.109
R469A
site-directed mutagenesis, exchange of conserved residue in the central loop, slightly reduced activity
Saccharomyces cerevisiae
2.4.1.109
R64 A
site-directed mutagenesis, exchange of conserved residue in the central loop, highly reduced activity
Saccharomyces cerevisiae
2.4.1.109
W253A
site-directed mutagenesis, exchange of conserved residue in the central loop, slightly reduced activity
Saccharomyces cerevisiae
Localization (protein specific)
EC Number
Localization
Commentary
Organism
GeneOntology No.
Textmining
2.4.1.109
endoplasmic reticulum
integral membrane protein
Saccharomyces cerevisiae
5783
-
2.4.1.109
membrane
integral, multiple transmembranal domains
Saccharomyces cerevisiae
16020
-
Natural Substrates/ Products (Substrates) (protein specific)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
2.4.1.109
dolichyl phosphate D-mannose + protein
Saccharomyces cerevisiae
-
dolichyl phosphate + O-D-mannosylprotein
-
-
-
2.4.1.109
dolichyl phosphate D-mannose + protein chitinase 1
Saccharomyces cerevisiae
PMT1
dolichyl phosphate + O-D-mannosylprotein chitinase 1
-
-
-
2.4.1.109
dolichyl phosphate D-mannose + protein Pir2/hsp150
Saccharomyces cerevisiae
PMT1
dolichyl phosphate + O-D-mannosylprotein Pir2/hsp150
-
-
-
Posttranslational Modification (protein specific)
EC Number
Posttranslational Modification
Commentary
Organism
2.4.1.109
glycoprotein
construction of diverse deletion mutants with different numbers of N-glycosylation sites; PMT1: 3 N-glycosylation sites
Saccharomyces cerevisiae
Specific Activity [micromol/min/mg] (protein specific)
EC Number
Specific Activity Minimum [Ámol/min/mg]
Specific Activity Maximum [Ámol/min/mg]
Commentary
Organism
2.4.1.109
additional information
-
wild-type and deletion mutants
Saccharomyces cerevisiae
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2.4.1.109
dolichyl phosphate D-mannose + Ac-Tyr-Ala-Thr-Ala-Val-NH2
PMT1
638342
Saccharomyces cerevisiae
dolichyl phosphate + O-D-mannosyl-Ac-Tyr-Ala-Thr-Ala-Val-NH2
-
638342
Saccharomyces cerevisiae
?
2.4.1.109
dolichyl phosphate D-mannose + protein
-
638342
Saccharomyces cerevisiae
dolichyl phosphate + O-D-mannosylprotein
-
-
-
-
2.4.1.109
dolichyl phosphate D-mannose + protein
-
638342
Saccharomyces cerevisiae
dolichyl phosphate + O-D-mannosylprotein
-
638342
Saccharomyces cerevisiae
?
2.4.1.109
dolichyl phosphate D-mannose + protein chitinase 1
PMT1
638342
Saccharomyces cerevisiae
dolichyl phosphate + O-D-mannosylprotein chitinase 1
-
-
-
-
2.4.1.109
dolichyl phosphate D-mannose + protein chitinase 1
PMT1
638342
Saccharomyces cerevisiae
dolichyl phosphate + O-D-mannosylprotein chitinase 1
-
638342
Saccharomyces cerevisiae
?
2.4.1.109
dolichyl phosphate D-mannose + protein Pir2/hsp150
PMT1
638342
Saccharomyces cerevisiae
dolichyl phosphate + O-D-mannosylprotein Pir2/hsp150
-
-
-
-
2.4.1.109
dolichyl phosphate D-mannose + protein Pir2/hsp150
PMT1
638342
Saccharomyces cerevisiae
dolichyl phosphate + O-D-mannosylprotein Pir2/hsp150
-
638342
Saccharomyces cerevisiae
?
Subunits (protein specific)
EC Number
Subunits
Commentary
Organism
2.4.1.109
More
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
Saccharomyces cerevisiae