Sequence of Cleavages in Temporary Inhibitors: Porcine Inhibitor Form II and Bovine Isoinhibitors A and C

Schneider, Sara L.; Stasiuk, L.; Laskowski, M.

doi:10.1007/978-3-642-87966-1_26

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Altered and Ruptured Scaffoldings1

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2005

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Cited by 3 publications

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“…While these are smaller than for BPTI, they are still huge drops in T m arising from a single peptide bond cleavage. In all 3 seco cases, when an attempt to determine K a was made at 23°C, there was evidence of strong "temporary inhibition" -a phenomenon where initial inhibition is followed by extensive enzymatic hydrolysis of the inhibitor, and release of the free enzyme [41]. This is not surprising since the T m values of these preparations are not very far from the temperature (23°C) of K a measurement.…”

Section: Altered and Ruptured Scaffoldingsmentioning

confidence: 81%

The Role of Scaffolding in Standard Mechanism Serine Proteinase Inhibitors

Kelly¹,

Laskowski²,

Qasim³

2005

PPL

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In single domain, "standard mechanism" protein inhibitors of serine proteinases, about a dozen residues make contact with the cognate enzyme. The remainder of the molecule, the scaffolding, holds the reactive site region of the inhibitor in a canonical conformation, improves the binding by about six orders of magnitude and protects it from proteolysis. However, the stability and global structure of the scaffolding is irrelevant to inhibition, provided that inhibition is measured much below the melting temperature, Tm.

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Section: Altered and Ruptured Scaffoldingsmentioning

confidence: 81%