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1 berculosis, primarily as a building block of mycothiol.
2 GlcNAc-Ins from the medium and convert it to mycothiol.
3 idase is highly specific for S-conjugates of mycothiol.
4 the cell and utilized in the resynthesis of mycothiol.
5 M. smegmatis at a level about twice that of mycothiol.
6 d by MtAhpE in the presence of MR, Mrx1, and mycothiol.
7 covalent adducts with N-acetyl-cysteine and mycothiol.
8 m reflected by the ratio of reduced/oxidized mycothiol.
9 am-positive bacteria lacking glutathione and mycothiol.
10 ion of radiolabeled inositol 1-phosphate and mycothiol.
13 The highly aerobic actinomycetes produce mycothiol, a conjugate of N-acetylcysteine with a pseudo
14 first enzyme involved in the biosynthesis of mycothiol, a major low-molecular-weight thiol in M. tube
16 n that a simplified cyclohexyl thioglycoside mycothiol analogue is a good substrate for MCA, it appea
17 onent correlated with defective recycling of mycothiol and accumulation of cellular oxidative damage.
18 cobacteria as a component of the major thiol mycothiol and also in the cell wall, with phosphatidylin
19 edoxin-1 (MtMrx1) acting in combination with mycothiol and mycothiol disulfide reductase (MR), as a b
22 peroxide detoxification actions inferred for mycothiol, and more recently, for Mrx1 in cellular syste
23 served that it demycothiolates and reduces a mycothiol arsenate adduct with kinetic properties differ
24 ermined by NMR the solution conformations of mycothiol bimane (MSmB) and the pseudodisaccharide 1-D-G
25 thiols, such as cysteine and an analogue of mycothiol, bind weakly to the [4Fe-4S] cluster, and expo
26 n of a chemical library of inhibitors of the mycothiol biosynthesis enzyme GlcNAc-Ins deacetylase (Ms
32 The mshA deletion mutants were defective in mycothiol biosynthesis, were only ethionamide-resistant
38 mycothiol-S-conjugate amidase (MCA) and the mycothiol biosynthetic enzyme D-GlcNAc-alpha-(1 --> 1)-D
39 in a sigR null mutant, although no candidate mycothiol biosynthetic genes were identified among the s
42 r four weeks showed a reduction in levels of mycothiol, but phosphatidylinositol mannoside, lipomanna
43 Rv1170, a homolog of Rv1082, possesses weak mycothiol conjugate amidase activity but shows substanti
44 l mycothiol-dependent detoxification enzyme, mycothiol conjugate amidase, was recently identified in
45 namycins (Gdms B-G, including new linear and mycothiol conjugates), were characterized as metabolites
46 cterium smegmatis shown to be GlcNAc-Ins and mycothiol deficient was sequenced to identify a putative
47 It was shown that GlcNAc-Ins is absent in mycothiol-deficient mutant strain 49 of M. smegmatis and
49 of (35)S methionine into the cysteine adduct mycothiol, demonstrated the conversion of exogenous meth
50 enzyme GlcNAc-Ins deacetylase (MshB) and the mycothiol-dependent detoxification enzyme mycothiol- S-c
51 hat represent the natural substrates for the mycothiol-dependent detoxification enzyme mycothiol-S-co
55 al analyses revealed that Rv2466c is a novel mycothiol-dependent reductase, which represents a mycore
58 x1) acting in combination with mycothiol and mycothiol disulfide reductase (MR), as a biologically re
60 dation of the two-electron reduced enzyme by mycothiol disulfide yielded a maximum rate of 190 +/- 10
61 in mshA demonstrate the non-essentiality of mycothiol for growth in vitro and in vivo, and provide a
64 The final three steps in the biosynthesis of mycothiol have been fully elucidated but the initial ste
65 intermediate in the biosynthetic pathway of mycothiol, i.e., 1-D-myo-inosityl-2-(N-acetyl-L-cysteiny
66 members of the Actinomycetes family produce mycothiol, i.e., 1-d-myo-inosityl-2-(N-acetyl-l-cysteiny
72 ciated with the membrane fraction, and since mycothiol is hydrophilic, direct reduction by MtMrx1 mig
78 ese studies establish for the first time how mycothiol metabolism is regulated to cope with stress fr
79 nstrated that Mca is highly specific for the mycothiol moiety of mycothiol S-conjugates and relativel
81 r members of the actinomycete family produce mycothiol (MSH or acetylcysteine-glucosamine-inositol, A
83 of Mycobacterium smegmatis does not produce mycothiol (MSH) and was found to markedly overproduce bo
84 hione and instead utilize the small molecule mycothiol (MSH) as their primary reducing agent and for
90 WhiB3, and the major M. tuberculosis thiol, mycothiol (MSH), are required to resist acidic stress du
91 or the determination of femtomole amounts of mycothiol (MSH), the main low-molecular-weight thiol in
93 omycetes do not produce glutathione but make mycothiol (MSH; AcCys-GlcN-Ins) that has functions simil
97 y; rather, it receives electrons through the mycothiol/mycothione reductase/NADPH pathway to activate
99 ase, MshA, is required for production of the mycothiol precursor, 1-O-(2-acetamido-2-deoxy-alpha-D-gl
103 e PknG mutant exhibited a reductive shift in mycothiol redox potential and compromised stress respons
104 onment resulted in higher oxidative shift in mycothiol redox potential of PknG mutant compared with t
107 These results indicate that mycothiol and mycothiol S-conjugate amidase play an important role in
109 Significant activity was also seen with the mycothiol S-conjugate of the antibiotic cerulenin as a s
110 highly specific for the mycothiol moiety of mycothiol S-conjugates and relatively nonspecific for th
111 gate amidase (Mca) cleaves the amide bond of mycothiol S-conjugates of a variety of alkylating agents
112 pathway utilizes the amidase (Mca) to cleave mycothiol S-conjugates to produce GlcN-Ins and a mercapt
113 n its ability to react with a broad range of mycothiol S-conjugates, including two different classes
114 he mycothiol-dependent detoxification enzyme mycothiol- S-conjugate amidase (MCA) from Mycobacterium
115 he mycothiol-dependent detoxification enzyme mycothiol-S-conjugate amidase (MCA) and the mycothiol bi
116 could be adapted to measure the activity of mycothiol-S-conjugate amidase, a metal-dependent amidase
120 tructure of the ternary complex reveals that mycothiol synthase undergoes a large conformational chan
121 ene disruption in the mshD gene that encodes mycothiol synthase, the final enzyme in MSH biosynthesis
122 om thioredoxin reductase (TrxR) and not from mycothiol, the low molecular weight thiol of actinomycet
123 g agent monobromobimane (mBBr), the cellular mycothiol was converted to its bimane derivative (MSmB).
125 evel of the major actinomycete thiol buffer, mycothiol, was fourfold lower in a sigR null mutant, alt
126 e glutathione but make an alternative thiol, mycothiol, which has functions similar to those of gluta
127 oxidized MtAhpE forms a mixed disulfide with mycothiol, which in turn is reduced by MtMrx1 using a mo
128 reaction, MsrA forms a mixed disulfide with mycothiol, which is transferred via a thiol disulfide re
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