Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary 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

Protein Variants

EC Number Protein Variants Comment 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 Comment 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 Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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 UniProt Comment Textmining
2.4.1.109 Saccharomyces cerevisiae
-
 gene PMT1
-
2.4.1.109 Saccharomyces cerevisiae
-
 gene PMT2
-

Posttranslational Modification

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

Reaction

EC Number Reaction Comment Organism Reaction ID
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
a

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.1.109 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
-
 ?
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 PMT1 Saccharomyces cerevisiae dolichyl phosphate + O-D-mannosylprotein chitinase 1
-
 ?
2.4.1.109 dolichyl phosphate D-mannose + protein Pir2/hsp150 PMT1 Saccharomyces cerevisiae dolichyl phosphate + O-D-mannosylprotein Pir2/hsp150
-
 ?

Subunits

EC Number Subunits Comment Organism
2.4.1.109 More topology model of PMT1 Saccharomyces cerevisiae
2.4.1.109 More PMT1 and PMT2 function as a complex Saccharomyces cerevisiae
2.4.1.109 More central hydrophilic loop is essential for catalytic activity, not complex formation, and is conserved throughout the PMT-family Saccharomyces cerevisiae
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 Saccharomyces cerevisiae

Synonyms

EC Number Synonyms Comment Organism
2.4.1.109 PMT
-
 Saccharomyces cerevisiae