3.5.1.115: mycothiol S-conjugate amidase
This is an abbreviated version!
For detailed information about mycothiol S-conjugate amidase, go to the full flat file.
Word Map on EC 3.5.1.115
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3.5.1.115
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tuberculosis
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actinomycetes
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deacetylase
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glcnac-ins
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mycothiol-dependent
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electrophilic
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mercapturic
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smegmatis
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amide
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monobromobimane
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n-acetylcysteine
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metalloprotein
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antimycobacterial
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cerulenin
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rifamycin
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text
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sponge
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alpha-helices
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deacetylation
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bromotyrosine
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accys
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medicine
- 3.5.1.115
- tuberculosis
- actinomycetes
- deacetylase
-
glcnac-ins
-
mycothiol-dependent
-
electrophilic
-
mercapturic
- smegmatis
- amide
- monobromobimane
- n-acetylcysteine
- metalloprotein
-
antimycobacterial
- cerulenin
- rifamycin
-
text
-
sponge
-
alpha-helices
-
deacetylation
-
bromotyrosine
-
accys
- medicine
Reaction
Synonyms
MCA, mycothiol S-conjugate amidase, Rv1082
ECTree
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General Information
General Information on EC 3.5.1.115 - mycothiol S-conjugate amidase
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evolution
malfunction
metabolism
physiological function
additional information
some Gram-positive bacteria, such as members of Corynebacterium, Mycobacterium, Rhodococcus and Streptomyces, cannot produce GSH but instead synthesize its functional equivalent, mycothiol
evolution
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some Gram-positive bacteria, such as members of Corynebacterium, Mycobacterium, Rhodococcus and Streptomyces, cannot produce GSH but instead synthesize its functional equivalent, mycothiol
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the Ami37 mutation in mca renders the mutant strain more susceptible to electrophilic toxins, such as N-ethylmalemide, iodoacetamide, and chlorodinitrobenzene, and to several oxidants, such as menadione and plumbagin. The mca mutant is also more susceptible to the antituberculous antibiotic streptomycin
malfunction
mutants lacking the enzyme and mycothiol are more susceptible to alkylating agents and oxidants, e.g. monobromobimane, iodoacetamide, N-ethylmaleimide, 1-chloro-2,4-dinitrobenzene, and methyllglyoxal, or to some macrolides and beta-lactams, e.g. rifamycin S, than the wild-type enzyme. Heavy metal ions, including Cd2+, Ni2+, Cr2+ and Cu2+, markedly inhibit growth of the mca mutant relative to the wild type strain
malfunction
Mycolicibacterium smegmatis mc(2)155 / ATCC 700084
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the Ami37 mutation in mca renders the mutant strain more susceptible to electrophilic toxins, such as N-ethylmalemide, iodoacetamide, and chlorodinitrobenzene, and to several oxidants, such as menadione and plumbagin. The mca mutant is also more susceptible to the antituberculous antibiotic streptomycin
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malfunction
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mutants lacking the enzyme and mycothiol are more susceptible to alkylating agents and oxidants, e.g. monobromobimane, iodoacetamide, N-ethylmaleimide, 1-chloro-2,4-dinitrobenzene, and methyllglyoxal, or to some macrolides and beta-lactams, e.g. rifamycin S, than the wild-type enzyme. Heavy metal ions, including Cd2+, Ni2+, Cr2+ and Cu2+, markedly inhibit growth of the mca mutant relative to the wild type strain
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mycothiol S-conjugate amidase plays an important role in the detoxification of alkylating agents and antibiotics
metabolism
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mycothiol serves as the primary reducing agent in Mycobacterium species, and is also a cofactor for the detoxification of xenobiotics. The enzyme catalyzes the cleavage of mycothiol-S-conjugates to form a mercapturic acid, which is excreted from the mycobacterium
metabolism
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mycothiol serves as the primary reducing agent in Mycobacterium species, and is also a cofactor for the detoxification of xenobiotics. The enzyme catalyzes the cleavage of mycothiol-S-conjugates to form a mercapturic acid, which is excreted from the mycobacterium
mycothiol S-conjugate amidase is a key enzyme involved in MSH-dependent detoxification. In detoxification process, mycothiol directly reacts with electrophilic compounds by its thiol moiety, forming MSH S-conjugates, regulation mechanism, potential roles of the enzyme in resistance to alkylating agents and oxidants and in the survival of Corynebacterium glutamicum by coping with multiple stresses and detoxifying toxins, overview
physiological function
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mycothiol S-conjugate amidase is a key enzyme involved in MSH-dependent detoxification. In detoxification process, mycothiol directly reacts with electrophilic compounds by its thiol moiety, forming MSH S-conjugates, regulation mechanism, potential roles of the enzyme in resistance to alkylating agents and oxidants and in the survival of Corynebacterium glutamicum by coping with multiple stresses and detoxifying toxins, overview
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residues Asp14, Tyr137, His139 and Asp141 are important for enzyme activity
additional information
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residues Asp14, Tyr137, His139 and Asp141 are important for enzyme activity
additional information
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residues Asp14, Tyr137, His139 and Asp141 are important for enzyme activity
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