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Literature summary for 3.4.24.27 extracted from

  • Liu, Y.H.; Konermann, L.
    Conformational dynamics of free and catalytically active thermolysin are indistinguishable by hydrogen/deuterium exchange mass spectrometry (2008), Biochemistry, 47, 6342-6351.
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Bacillus thermoproteolyticus
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Reaction

Reaction Comment Organism Reaction ID
preferential cleavage: -/-Leu > -/-Phe substrate turnover is associated with hinge bending that leads to a closed conformation. Product release regenerates the open form, such that steady-state catalysis involves a continuous closing/opening cycle. Elements in the periphery of the two lobes are most mobile. These peripheral regions undergo quite pronounced structural changes during the catalytic cycle. In contrast, active site residues exhibit only a moderate degree of backbone flexibility, and the central zinc appears to be in a fairly rigid environment. The hydrogen/deuterium exchange behavior of catalytically active thermolysin is indistinguishable from that of the free enzyme Bacillus thermoproteolyticus