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Literature summary for 3.4.11.18 extracted from

  • Reddi, R.; Arya, T.; Kishor, C.; Gumpena, R.; Ganji, R.J.; Bhukya, S.; Addlagatta, A.
    Selective targeting of the conserved active site cysteine of Mycobacterium tuberculosis methionine aminopeptidase with electrophilic reagents (2014), FEBS J., 281, 4240-4248.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
wild-type enzyme crystals are soaked with N-ethylmaleimide, 2-hydroxyethyl disulfide, and methyl homocysteine disulfide. Crystal structure determined in the presence of cobalt chloride shows electron density for the mercaptoethanol covalently linked to Cys105. However, in the absence of cobalt chloride, the whole 2-hydroxyethyl disulfide molecule is observed in the S1 pocket without any covalent modification. Metal ions in the active site assist in the covalent modification of Cys105 by orienting the reagents appropriately for a successful reaction Mycobacterium tuberculosis

Protein Variants

Protein Variants Comment Organism
C105S contratry to wild-type, no inhibition by cysteien-modifying compounds N-ethylmaleimide, 5,5'-dithiobis(2-nitrobenzoic acid) and 2-hydroxyethyl disulfide Mycobacterium tuberculosis

Inhibitors

Inhibitors Comment Organism Structure
2-hydroxyethyl disulfide inhibition is through covalent modifiction of residue C105 Mycobacterium tuberculosis
5,5'-dithiobis(2-nitrobenzoic acid) inhibition is through covalent modifiction of residue C105 Mycobacterium tuberculosis
N-ethylmaleimide 1 mM, 90% inhibition. Inhibition is through covalent modifiction of residue C105 Mycobacterium tuberculosis

Organism

Organism UniProt Comment Textmining
Mycobacterium tuberculosis P9WK19
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-
Mycobacterium tuberculosis ATCC 25618 P9WK19
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-

Synonyms

Synonyms Comment Organism
MetAP1c
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Mycobacterium tuberculosis
methionine aminopeptidase 2
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Mycobacterium tuberculosis