Target intelligence / Profile preview

Zinc metalloproteinase aureolysin

Molecular classification
Enzyme, Metalloproteinase, Zinc-dependent proteinase, Thermolysin-like proteinase
01

Overview

Zinc metalloproteinase aureolysin is a secreted extracellular metalloprotease from *Staphylococcus aureus*, belonging to the thermolysin/M4 family of zinc-dependent proteinases[3]. The mature enzyme consists of a 301-amino acid catalytic domain processed from a larger precursor, and binds one zinc and up to three calcium ions for activity and structural integrity[1][3]. Aureolysin can degrade host plasma proteinase inhibitors, activate prothrombin, modulate immune responses, and process other bacterial proteins, playing an essential role in the virulence and immune evasion capacity of *S. aureus*[1][2][4]. While widely accepted as a bacterial virulence factor and potential therapeutic target, there are currently no approved clinical inhibitors specific to aureolysin[3][4].

Other names
aureolysinaurStaphylococcal aureolysinStaphylococcus aureus metalloproteinase
02

Mechanism of action

Metal chelation (inhibition by removal/blocking of catalytic zinc/cofactor); Protease inhibition (blocking the active site or substrate access)[3]

03

Biological functions

Proteolysis of host and bacterial proteinsImmune evasion (resistance to complement-mediated killing)Activation and processing of staphylococcal secreted proteinsDirect effect on host cell surface receptor shedding[2][4]
04

Disease associations

Infection (Staphylococcal infection/virulence factor)Inflammation (indirect roles via immune modulation)[2][4]
05

Safety considerations

Potential bacterial resistance if used as an antibacterial targetHomology to human metalloproteinases—possible off-target toxicity/challenges in developing highly specific inhibitors[3]
06

Interacting drugs

Ethylenediaminetetraacetic acid (EDTA) (general metalloproteinase inhibitor; not clinically specific)

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