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Literature summary for 2.4.1.109 extracted from

  • Nett, J.H.; Cook, W.J.; Chen, M.T.; Davidson, R.C.; Bobrowicz, P.; Kett, W.; Brevnova, E.; Potgieter, T.I.; Mellon, M.T.; Prinz, B.; Choi, B.K.; Zha, D.; Burnina, I.; Bukowski, J.T.; Du, M.; Wildt, S.; Hamilton, S.R.
    Characterization of the Pichia pastoris protein-O-mannosyltransferase gene family (2013), PLoS ONE, 8, e68325.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.4.1.109

Cloned(Commentary)

Cloned (Comment) Organism
gene PAS_chr2-1_0212, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, subcloning in Escherichia coli strain DH5alpha Komagataella pastoris
gene PAS_chr2-1_0256, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, subcloning in Escherichia coli strain DH5alpha Komagataella pastoris

Protein Variants

Protein Variants Comment Organism
additional information construction of Pichia pastoris single and all PMT knockout mutant strains, the DELTApmt1 and DELTApmt2 strains secrete protein with significantly reduced O-glycan site occupancy Komagataella pastoris

Inhibitors

Inhibitors Comment Organism Structure
5-[[(3-(1-phenyl-2-hydroxy)ethoxy)-4-(2-phenylethoxy)phenyl]methylene]-4-oxo-2-thioxo-3-thiazolidine acetic acid i.e. PMTi-3, inhibits PMT enzymes Komagataella pastoris
5-[[(3-(1-phenyl-2-hydroxy)ethoxy)-4-(2-phenylethoxy)phenyl]methylene]-4-oxo-2-thioxo-3-thiazolidineacetic acid i.e. PMTi-3, inhibits PMT enzymes Komagataella pastoris
5-[[3,4-bis(phenylmethoxy)phenyl]methylene]-4-oxo-2-thioxo-3-thiazolidine acetic acid i.e. PMTi-1, inhibits PMT enzymes Komagataella pastoris
5-[[3,4-bis(phenylmethoxy)phenyl]methylene]-4-oxo-2-thioxo-3-thiazolidineacetic acid i.e. PMTi-1, inhibits PMT enzymes Komagataella pastoris
additional information inhibitor synthesis, overview; inhibitor synthesis, overview Komagataella pastoris

Localization

Localization Comment Organism GeneOntology No. Textmining
endoplasmic reticulum
-
 Komagataella pastoris 5783
-

Organism

Organism UniProt Comment Textmining
Komagataella pastoris C4QZZ6 formerly Pichia pastoris, several strains, gene PAS_chr2-1_0212, isozyme PMT1
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Komagataella pastoris C4R044 formerly Pichia pastoris, several strains, gene PAS_chr2-1_0256, isozyme PMT2
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Komagataella pastoris GS115 C4QZZ6 formerly Pichia pastoris, several strains, gene PAS_chr2-1_0212, isozyme PMT1
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Komagataella pastoris GS115 C4R044 formerly Pichia pastoris, several strains, gene PAS_chr2-1_0256, isozyme PMT2
-

Synonyms

Synonyms Comment Organism
PMT1
-
 Komagataella pastoris
PMT2
-
 Komagataella pastoris
protein-Omannosyltransferase
-
 Komagataella pastoris

General Information

General Information Comment Organism
evolution the enzyme is a member of the protein-O-mannosyltransferase (PMT) family. Pichia pastoris has five PMT genes. Based on sequence homology, the PMTs can be grouped into three subfamilies, with both PMT1 and PMT2 subfamilies possessing two members each (PMT1 and PMT5, and PMT2 and PMT6, respectively). The remaining subfamily, PMT4, has only one member, PMT4. PMT1 and PMT2 each play a significant role in O-glycosylation Komagataella pastoris
malfunction PMT2 knockout, and to a lesser extent a PMT1 knockout, in addition to a reduction in O-glycan site occupancy also leads to shortened O-glycan chain lengths Komagataella pastoris
physiological function protein O-mannosylation in fungi is initiated at the endoplasmic reticulum by a family of protein-O-mannosyltransferases that transfer mannose from dolichyl phosphate-activated mannose to serine or threonine residues of proteins entering the endoplasmic reticulum Komagataella pastoris