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Literature summary for 2.4.1.346 extracted from

  • Guerin, M.E.; Kaur, D.; Somashekar, B.S.; Gibbs, S.; Gest, P.; Chatterjee, D.; Brennan, P.J.; Jackson, M.
    New insights into the early steps of phosphatidylinositol mannoside biosynthesis in mycobacteria: PimB is an essential enzyme of Mycobacterium smegmatis (2009), J. Biol. Chem., 284, 25687-25696.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.4.1.346

Activating Compound

Activating Compound Comment Organism Structure
isopropyl-1-thio-beta-D-galactopyranoside
-
 Mycolicibacterium smegmatis

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli BL21 Mycolicibacterium smegmatis

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane
-
 Mycolicibacterium smegmatis 16020
-

Organism

Organism UniProt Comment Textmining
Mycolicibacterium smegmatis A0R043
-
-
Mycolicibacterium smegmatis ATCC 700084 A0R043
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Mycolicibacterium smegmatis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
GDP-alpha-D-mannose + 2-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
-
 Mycolicibacterium smegmatis GDP + 2,6-di-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
-
 ?
GDP-alpha-D-mannose + 2-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
-
 Mycolicibacterium smegmatis ATCC 700084 GDP + 2,6-di-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
-
 ?
GDP-Man + phosphatidyl-myo-inositol assay at pH 7.5, 37°C, reaction stopped with CHCl3/CH3OH Mycolicibacterium smegmatis ?
-
 ?
GDP-Man + phosphatidyl-myo-inositol assay at pH 7.5, 37°C, reaction stopped with CHCl3/CH3OH Mycolicibacterium smegmatis ATCC 700084 ?
-
 ?
additional information PimB specifically catalyzes the transfer of a mannopyranosyl residue to the 6-position of the myo-inositol ring of phosphatidylinositol Mycolicibacterium smegmatis ?
-
 ?
additional information PimB specifically catalyzes the transfer of a mannopyranosyl residue to the 6-position of the myo-inositol ring of phosphatidylinositol Mycolicibacterium smegmatis ATCC 700084 ?
-
 ?

Synonyms

Synonyms Comment Organism
mannoslytransferase PimB'
-
 Mycolicibacterium smegmatis
MSMEG_4253
-
 Mycolicibacterium smegmatis
PimB
-
 Mycolicibacterium smegmatis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Mycolicibacterium smegmatis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 assay at Mycolicibacterium smegmatis

General Information

General Information Comment Organism
physiological function both mannosyltransferases PimA and PimB' (MSMEG_4253) recognize phosphatidyl-myo-inositol as a lipid acceptor. PimA specifically catalyzes the transfer of a mannopyranosyl residue to the 2-position of the myo-inositol ring of phosphatidylinositol, whereas PimB' exclusively transfers to the 6-position. PimB' can catalyze the transfer of a mannopyranosyl residue onto the phosphatidylinositol-monomannoside (PIM1) product of PimA, while PimA is unable in vitro to transfer mannopyranosyl onto the PIM1 product of PimB' Mycolicibacterium smegmatis