Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.4.21.B48 extracted from

  • Yao, J.; Wlodawer, A.; Guo, H.
    Understanding the autocatalytic process of pro-kumamolisin activation from molecular dynamics and quantum mechanical/molecular mechanical (QM/MM) free-energy simulations (2013), Chem. Eur. J., 19, 10849-10852.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.21.B48

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structure analysis Bacillus sp. (in: Bacteria)

Protein Variants

Protein Variants Comment Organism
S278A an inactive pro-kumamolisin mutant, the catalytic domain of the mutant exhibits a virtually identical structure compared to the active enzyme Bacillus sp. (in: Bacteria)

Organism

Organism UniProt Comment Textmining
Bacillus sp. (in: Bacteria) Q8RR56
-
-
Bacillus sp. (in: Bacteria) MN-32 Q8RR56
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification the enzyme performs autoactivation, autocatalytic process of pro-kumamolisin activation, the protonation of Asp164 triggers conformational changes and generates the functional active site for autocatalysis, mechanism of acylation for autocatalytic cleavage of prodomain, molecular dynamics and quantum mechanical/molecular mechanical free-energy simulations, overview Bacillus sp. (in: Bacteria)

Synonyms

Synonyms Comment Organism
kumamolisin
-
 Bacillus sp. (in: Bacteria)

General Information

General Information Comment Organism
evolution kumamolisin belongs to the family of serine-carboxyl peptidases, i.e. sedolisins Bacillus sp. (in: Bacteria)
additional information one of the reasons for sedolisins to use an aspartate as a catalyst (e.g., Asp164 in kumamolisin) instead of asparagine (the oxyanion-hole residue in classical serine peptidase) might be due in part to the requirement for the creation of a built-in switch that delays the self-activation until secretion into acidic medium. The X-ray structure of the S278A pro-kumamolisin mutant is used to generate the model for the wild-type pro-kumamolisin through a manual change of Ala278 to Ser278 Bacillus sp. (in: Bacteria)