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Literature summary extracted from

  • Kocabas, E.; Liu, H.; Hernick, M.
    Identity of cofactor bound to mycothiol conjugate amidase (Mca) influenced by expression and purification conditions (2015), Biometals, 28, 755-763 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.5.1.115 the gene is cloned into the pVP56 K [N-terminal His-maltose-binding protein (MBP)] and pFN18 K (N-terminal Halo-tag) expression vectors, expression in Escherichia coli BL21(DE3) cells Mycolicibacterium smegmatis
3.5.1.115 the gene is cloned into the pVP56 K [N-terminal His-maltose-binding protein (MBP)] and pFN18 K (N-terminal Halo-tag) expression vectors, expression in Escherichia coli BL21(DE3) cells Mycobacterium tuberculosis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.5.1.115 Fe2+ 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 Mycolicibacterium smegmatis
3.5.1.115 Fe2+ 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 Mycobacterium tuberculosis
3.5.1.115 Zn2+ 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 Mycolicibacterium smegmatis
3.5.1.115 Zn2+ 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 Mycobacterium tuberculosis

Organism

EC Number Organism UniProt Comment Textmining
3.5.1.115 Mycobacterium tuberculosis
-
-
-
3.5.1.115 Mycolicibacterium smegmatis
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.5.1.115
-
 Mycolicibacterium smegmatis
3.5.1.115
-
 Mycobacterium tuberculosis

Synonyms

EC Number Synonyms Comment Organism
3.5.1.115 MCA
-
 Mycolicibacterium smegmatis
3.5.1.115 MCA
-
 Mycobacterium tuberculosis

General Information

EC Number General Information Comment Organism
3.5.1.115 metabolism 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 Mycolicibacterium smegmatis
3.5.1.115 metabolism 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 Mycobacterium tuberculosis