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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Metals Ions
Metals Ions on EC 3.5.1.115 - mycothiol S-conjugate amidase
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Ca2+
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the protein contains 2.6 equivalents of Ca2+ per subunit after purification
Fe2+
Zn2+
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metalloamidase. The enzyme purifies with (stoichiometric) Fe2+ when purified under anaerobic conditions, and Zn2+ when purified under aerobic conditions. It is likely a Fe2+-dependent enzyme under physiological conditions, with Zn2+-enzyme an experimental artifact that can become biologically relevant under oxidatively stressed conditions
Fe2+
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metalloamidase. The enzyme purifies with (stoichiometric) Fe2+ when purified under anaerobic conditions, and Zn2+ when purified under aerobic conditions. It is likely a Fe2+-dependent enzyme under physiological conditions, with Zn2+-enzyme an experimental artifact that can become biologically relevant under oxidatively stressed conditions
Zn2+
-
the protein contains 1.4 equivalents of Zn2+ per subunit after purification
Zn2+
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metalloamidase. The enzyme purifies with (stoichiometric) Fe2+ when purified under anaerobic conditions, and Zn2+ when purified under aerobic conditions. It is likely a Fe2+-dependent enzyme under physiological conditions, with Zn2+-enzyme an experimental artifact that can become biologically relevant under oxidatively stressed conditions
Zn2+
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metalloamidase. The enzyme purifies with (stoichiometric) Fe2+ when purified under anaerobic conditions, and Zn2+ when purified under aerobic conditions. It is likely a Fe2+-dependent enzyme under physiological conditions, with Zn2+-enzyme an experimental artifact that can become biologically relevant under oxidatively stressed conditions