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Literature summary for 2.4.1.289 extracted from

  • Mills, J.A.; Motichka, K.; Jucker, M.; Wu, H.P.; Uhlik, B.C.; Stern, R.J.; Scherman, M.S.; Vissa, V.D.; Pan, F.; Kundu, M.; Ma, Y.F.; McNeil, M.
    Inactivation of the mycobacterial rhamnosyltransferase, which is needed for the formation of the arabinogalactan-peptidoglycan linker, leads to irreversible loss of viability (2004), J. Biol. Chem., 279, 43540-43546.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
gene wbbL, expression in and complementation of Mycobacterium smegmatis strain mc2155 temperature-sensitive mutant 2-20/32 Escherichia coli
orf Rv3265c or gene wbbL, expression in and complementation of Mycobacterium smegmatis strain mc2155 temperature-sensitive mutant 2-20/32, the enzyme also is capable of restoring an Escherichia coli K12 strain containing an insertionally inactivated wbbL to O-antigen positive, functional expression from plasmid in Escherichia coli strain K12 EMG2 Mycobacterium tuberculosis

Protein Variants

Protein Variants Comment Organism
additional information the Escherichia coli mutant strain K12 EMG2 contains an insertionally inactivated wbbL and is devoid of any O-antigen and shows no WbbL activity, complementation by expression of WbbL from Mycobacterium tuberculosis, a plasmid encoding the putative rhamnosyltransferase gene from Mycobacterium tuberculosis also results in O-antigen synthesis Escherichia coli
additional information the temperature-sensitive mutant contains a single-base change that has a proline changed to a serine residue. Exposure of in mc2155 mutant 2-20/32 to higher non-permissive temperatures results in bacteria that cannot be recovered at the lower permissive temperatures. Complementation of the mutants strain by expression of gene wbbL from Escherichia coli or Mycobacterium tuberculosis Mycolicibacterium smegmatis

Organism

Organism UniProt Comment Textmining
Escherichia coli P36667 gene wbbL
-
Escherichia coli WG1 P36667 gene wbbL
-
Mycobacterium tuberculosis P9WMY3 orf Rv3265c, gene wbbL
-
Mycobacterium tuberculosis H37Rv P9WMY3 orf Rv3265c, gene wbbL
-
Mycolicibacterium smegmatis Q9RN49 a temperature-sensitive mutant strain 2-20/32, gene wbbL
-
Mycolicibacterium smegmatis mc(2)155 / ATCC 700084 Q9RN49 a temperature-sensitive mutant strain 2-20/32, gene wbbL
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
dTDP-beta-L-rhamnose + GlcNAc-diphospho-trans,octacis-decaprenol
-
Mycobacterium tuberculosis ?
-
?
dTDP-beta-L-rhamnose + GlcNAc-diphospho-trans,octacis-decaprenol
-
Mycobacterium tuberculosis H37Rv ?
-
?

Synonyms

Synonyms Comment Organism
dTDP-Rha:alpha-D-GlcNAc-pyrophosphate polyprenol, alpha-3-L-rhamnosyltransferase
-
Mycobacterium tuberculosis
dTDP-Rha:alpha-D-GlcNAc-pyrophosphate polyprenol, alpha-3-L-rhamnosyltransferase
-
Mycolicibacterium smegmatis
dTDP-Rha:alpha-D-GlcNAc-pyrophosphate polyprenol, alpha-3-L-rhamnosyltransferase
-
Escherichia coli
WbbL
-
Mycobacterium tuberculosis
WbbL
-
Mycolicibacterium smegmatis
WbbL
-
Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Mycobacterium tuberculosis
37
-
assay at Mycolicibacterium smegmatis
37
-
assay at Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
assay at Mycobacterium tuberculosis
8
-
assay at Mycolicibacterium smegmatis
8
-
assay at Escherichia coli

General Information

General Information Comment Organism
malfunction the temperature-sensitive mc2155 strain 2-20/32 mutant shows loss of this transferase activity in 2-20/32 at elevated temperatures, complementation by expression of the enzyme encoded by genes wbbL from Escherichia coli and froms Mycobacterium tuberculosis Mycolicibacterium smegmatis
physiological function the enzyme is required for the rhamnosyl-L-containing linker unit responsible for the attachment of the cell wall polymer mycolyl-arabinogalactan to the peptidoglycan in mycobacteria Mycobacterium tuberculosis