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Literature summary for 2.4.1.109 extracted from

  • Girrbach, V.; Zeller, T.; Priesmeier, M.; Strahl-Bolsinger, S.
    Structure-function analysis of the dolichyl phosphate-mannose:protein O-mannosyltransferase ScPmt1p (2000), J. Biol. Chem., 275, 19288-19296.
    View publication on PubMed
Search for more literature for 2.4.1.109

Protein Variants

Protein Variants Comment Organism
D96A site-directed mutagenesis, exchange of conserved residue in the central loop, reduced activity Saccharomyces cerevisiae
E78A site-directed mutagenesis, exchange of conserved residue in the central loop, highly reduced activity Saccharomyces cerevisiae
H346A/H348A site-directed mutagenesis, exchange of conserved residue in the central loop, reduced activity Saccharomyces cerevisiae
H411A site-directed mutagenesis, exchange of conserved residue in the central loop, slightly reduced activity Saccharomyces cerevisiae
H472A site-directed mutagenesis, exchange of conserved residue in the central loop, reduced activity Saccharomyces cerevisiae
K234A site-directed mutagenesis, exchange of conserved residue in the central loop, slightly reduced activity Saccharomyces cerevisiae
L399A site-directed mutagenesis, exchange of conserved residue in the central loop, reduced activity Saccharomyces cerevisiae
L408A site-directed mutagenesis, exchange of conserved residue in the central loop, highly reduced activity Saccharomyces cerevisiae
L408A/H411A site-directed mutagenesis, exchange of conserved residue in the central loop, highly reduced activity Saccharomyces cerevisiae
additional information construction of diverse deletion mutants of PMT1, effect on activity and complex formation with PMT2, overview Saccharomyces cerevisiae
N370A site-directed mutagenesis, exchange of conserved residue in the central loop, slightly reduced activity Saccharomyces cerevisiae
Q359A/Q360A site-directed mutagenesis, exchange of conserved residue in the central loop, reduced activity Saccharomyces cerevisiae
Q493A/E495A site-directed mutagenesis, exchange of conserved residue in the central loop, reduced activity Saccharomyces cerevisiae
R138A site-directed mutagenesis, exchange of conserved residue in the central loop, highly reduced activity Saccharomyces cerevisiae
R398A site-directed mutagenesis, exchange of conserved residue in the central loop, reduced activity Saccharomyces cerevisiae
R469A site-directed mutagenesis, exchange of conserved residue in the central loop, slightly reduced activity Saccharomyces cerevisiae
R64 A site-directed mutagenesis, exchange of conserved residue in the central loop, highly reduced activity Saccharomyces cerevisiae
W253A site-directed mutagenesis, exchange of conserved residue in the central loop, slightly reduced activity Saccharomyces cerevisiae

Localization

Localization Comment Organism GeneOntology No. Textmining
endoplasmic reticulum integral membrane protein Saccharomyces cerevisiae 5783
-
membrane integral, multiple transmembranal domains Saccharomyces cerevisiae 16020
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
dolichyl phosphate D-mannose + protein Saccharomyces cerevisiae
-
 dolichyl phosphate + O-D-mannosylprotein
-
 ?
dolichyl phosphate D-mannose + protein chitinase 1 Saccharomyces cerevisiae PMT1 dolichyl phosphate + O-D-mannosylprotein chitinase 1
-
 ?
dolichyl phosphate D-mannose + protein Pir2/hsp150 Saccharomyces cerevisiae PMT1 dolichyl phosphate + O-D-mannosylprotein Pir2/hsp150
-
 ?

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
 gene PMT1
-
Saccharomyces cerevisiae
-
 gene PMT2
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein construction of diverse deletion mutants with different numbers of N-glycosylation sites Saccharomyces cerevisiae
glycoprotein PMT1: 3 N-glycosylation sites Saccharomyces cerevisiae

Reaction

Reaction Comment Organism Reaction ID
dolichyl beta-D-mannosyl phosphate + L-threonyl-[protein] = dolichyl phosphate + 3-O-(alpha-D-mannosyl)-L-threonyl-[protein] structure-function analysis Saccharomyces cerevisiae
a

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
 wild-type and deletion mutants Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
dolichyl phosphate D-mannose + Ac-Tyr-Ala-Thr-Ala-Val-NH2 PMT1 Saccharomyces cerevisiae dolichyl phosphate + O-D-mannosyl-Ac-Tyr-Ala-Thr-Ala-Val-NH2
-
 ?
dolichyl phosphate D-mannose + protein
-
 Saccharomyces cerevisiae dolichyl phosphate + O-D-mannosylprotein
-
 ?
dolichyl phosphate D-mannose + protein chitinase 1 PMT1 Saccharomyces cerevisiae dolichyl phosphate + O-D-mannosylprotein chitinase 1
-
 ?
dolichyl phosphate D-mannose + protein Pir2/hsp150 PMT1 Saccharomyces cerevisiae dolichyl phosphate + O-D-mannosylprotein Pir2/hsp150
-
 ?

Subunits

Subunits Comment Organism
More topology model of PMT1 Saccharomyces cerevisiae
More PMT1 and PMT2 function as a complex Saccharomyces cerevisiae
More central hydrophilic loop is essential for catalytic activity, not complex formation, and is conserved throughout the PMT-family Saccharomyces cerevisiae
More Arg138 is crucial for complex formation between PMT1 and PMT2, N-terminal third of the protein is essential for complex formation Saccharomyces cerevisiae

Synonyms

Synonyms Comment Organism
PMT
-
 Saccharomyces cerevisiae