Enzymes
UniProtKB help_outline | 3 proteins |
Enzyme class help_outline |
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- Name help_outline α-L-rhamnosyl-(1→3)-N-acetyl-α-D-glucosaminyl-diphospho-trans,octa-cis-decaprenol Identifier CHEBI:67209 Charge -2 Formula C64H105NO16P2 InChIKeyhelp_outline LTCQFZLIKIMFIG-DRJIPIRHSA-L SMILEShelp_outline C[C@@H]1O[C@@H](O[C@H]2[C@H](O)[C@@H](CO)O[C@H](OP([O-])(=O)OP([O-])(=O)OC\C=C(\C)CC\C=C(\C)CC\C=C(\C)CC\C=C(\C)CC\C=C(\C)CC\C=C(\C)CC\C=C(\C)CC\C=C(\C)CC\C=C(/C)CCC=C(C)C)[C@@H]2NC(C)=O)[C@H](O)[C@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 3 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline UDP-α-D-galactofuranose Identifier CHEBI:66915 Charge -2 Formula C15H22N2O17P2 InChIKeyhelp_outline ZQLQOXLUCGXKHS-SIAUPFDVSA-L SMILEShelp_outline [H][C@]1(O[C@H](OP([O-])(=O)OP([O-])(=O)OC[C@H]2O[C@H]([C@H](O)[C@@H]2O)n2ccc(=O)[nH]c2=O)[C@H](O)[C@H]1O)[C@H](O)CO 2D coordinates Mol file for the small molecule Search links Involved in 5 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline β-D-galactofuranosyl-(1→5)-β-D-galactofuranosyl-(1→4)-α-L-rhamnosyl-(1→3)-N-acetyl-α-D-glucosaminyl-diphospho-trans,octa-cis-decaprenol Identifier CHEBI:67210 Charge -2 Formula C76H125NO26P2 InChIKeyhelp_outline RUVOVZNNKIXXAL-ZVNAIUDSSA-L SMILEShelp_outline [H][C@]1(O[C@@H](O[C@H](CO)[C@]2([H])O[C@@H](O[C@H]3[C@H](C)O[C@@H](O[C@H]4[C@H](O)[C@@H](CO)O[C@H](OP([O-])(=O)OP([O-])(=O)OC\C=C(\C)CC\C=C(\C)CC\C=C(\C)CC\C=C(\C)CC\C=C(\C)CC\C=C(\C)CC\C=C(\C)CC\C=C(\C)CC\C=C(/C)CCC=C(C)C)[C@@H]4NC(C)=O)[C@H](O)[C@@H]3O)[C@H](O)[C@H]2O)[C@H](O)[C@H]1O)[C@H](O)CO 2D coordinates Mol file for the small molecule Search links Involved in 3 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H+ Identifier CHEBI:15378 Charge 1 Formula H InChIKeyhelp_outline GPRLSGONYQIRFK-UHFFFAOYSA-N SMILEShelp_outline [H+] 2D coordinates Mol file for the small molecule Search links Involved in 9,431 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline UDP Identifier CHEBI:58223 Charge -3 Formula C9H11N2O12P2 InChIKeyhelp_outline XCCTYIAWTASOJW-XVFCMESISA-K SMILEShelp_outline O[C@@H]1[C@@H](COP([O-])(=O)OP([O-])([O-])=O)O[C@H]([C@@H]1O)n1ccc(=O)[nH]c1=O 2D coordinates Mol file for the small molecule Search links Involved in 576 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
RHEA:34379 | RHEA:34380 | RHEA:34381 | RHEA:34382 | |
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Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Publications
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Identification of a novel galactosyl transferase involved in biosynthesis of the mycobacterial cell wall.
Mikusova K., Belanova M., Kordulakova J., Honda K., McNeil M.R., Mahapatra S., Crick D.C., Brennan P.J.
The possibility of the Rv3782 protein of Mycobacterium tuberculosis being a putative galactosyl transferase (GalTr) implicated in galactan synthesis arose from its similarity to the known GalTr Rv3808c, its classification as a nucleotide sugar-requiring inverting glycosyltransferase (GT-2 family), ... >> More
The possibility of the Rv3782 protein of Mycobacterium tuberculosis being a putative galactosyl transferase (GalTr) implicated in galactan synthesis arose from its similarity to the known GalTr Rv3808c, its classification as a nucleotide sugar-requiring inverting glycosyltransferase (GT-2 family), and its location within the "possible arabinogalactan biosynthetic gene cluster" of M. tuberculosis. In order to study the function of the enzyme, active membrane and cell wall fractions from Mycobacterium smegmatis containing the overexpressed Rv3782 protein were incubated with endogenous decaprenyldiphosphoryl-N-acetylglucosaminyl-rhamnose (C(50)-P-P-GlcNAc-Rha) as the primary substrate for galactan synthesis and UDP-[(14)C]galactopyranose as the immediate precursor of UDP-[(14)C]galactofuranose, the ultimate source of all of the galactofuranose (Galf) units of galactan. Obvious increased and selective synthesis of C(50)-P-P-GlcNAc-Rha-Galf-Galf, the earliest product in the pathway leading to the fully polymerized galactan, was observed, suggesting that Rv3782 encodes a GalTr involved in the first stages of galactan synthesis. Time course experiments pointed to a possible bifunctional enzyme responsible for the initial synthesis of C(50)-P-P-GlcNAc-Rha-Galf, followed by immediate conversion to C(50)-P-P-GlcNAc-Rha-Galf-Galf. Thus, Rv3782 appears to be the initiator of galactan synthesis, while Rv3808c continues with the subsequent polymerization events. << Less
J. Bacteriol. 188:6592-6598(2006) [PubMed] [EuropePMC]
This publication is cited by 2 other entries.
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Galactosyl transferases in mycobacterial cell wall synthesis.
Belanova M., Dianiskova P., Brennan P.J., Completo G.C., Rose N.L., Lowary T.L., Mikusova K.
Two galactosyl transferases can apparently account for the full biosynthesis of the cell wall galactan of mycobacteria. Evidence is presented based on enzymatic incubations with purified natural and synthetic galactofuranose (Galf) acceptors that the recombinant galactofuranosyl transferase, GlfT1 ... >> More
Two galactosyl transferases can apparently account for the full biosynthesis of the cell wall galactan of mycobacteria. Evidence is presented based on enzymatic incubations with purified natural and synthetic galactofuranose (Galf) acceptors that the recombinant galactofuranosyl transferase, GlfT1, from Mycobacterium smegmatis, the Mycobacterium tuberculosis Rv3782 ortholog known to be involved in the initial steps of galactan formation, harbors dual beta-(1-->4) and beta-(1-->5) Galf transferase activities and that the product of the enzyme, decaprenyl-P-P-GlcNAc-Rha-Galf-Galf, serves as a direct substrate for full polymerization catalyzed by another bifunctional Galf transferase, GlfT2, the Rv3808c enzyme. << Less
J. Bacteriol. 190:1141-1145(2008) [PubMed] [EuropePMC]
This publication is cited by 2 other entries.
Comments
Multi-step reaction: RHEA:34383 and RHEA:34387.