Literature summary for 3.4.21.5 extracted from

Sutherland, J.S.; Bhakta, V.; Filion, M.L.; Sheffield, W.P.
The transferable tail: fusion of the N-terminal acidic extension of heparin cofactor II to alpha1-proteinase inhibitor M358R specifically increases the rate of thrombin inhibition (2006), Biochemistry, 45, 11444-11452.

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Protein Variants

Protein Variants	Comment	Organism
additional information	fusion of the N-terminal acidic extension, residues 1-75, of heparin cofactor II to alpha1-proteinase inhibitor M358R to the enzyme specifically increases the rate of thrombin inhibition by 6fold, the mutant is termed HAPI M358R, maximal enhancement of alpha1-PI M358R activity requires the acidic residues between HCII residues 55 and 75, because no enhancement is observed either by fusion of residues 1-54 alone or by fusion of a mutated HCII acidic extension in which all Glu and Asp residues between positions 55 and 75 are neutralized by mutation, overview	Homo sapiens

Inhibitors

Inhibitors	Comment	Organism	Structure
heparin cofactor II	HCII, i.e. alpha1-antitrypsin, a serpin cofactor, contains a unique N-terminal extension that binds thrombin exosite 1, the mutant M358R is more active in inhibition of thrombin than the wild-type protein, maximal enhancement of alpha1-PI M358R activity requires the acidic residues between HCII residues 55 and 75	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	-	-

Synonyms

Synonyms	Comment	Organism
alpha-thrombin	-	Homo sapiens

Ki Value [mM]

Ki Value [mM]	Ki Value maximum [mM]	Inhibitor	Comment	Organism	Structure
additional information	-	additional information	inhibition kinetics	Homo sapiens

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Release 2023.1 (January 2023)