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This research investigates how specific amino acid residues in tissue-type plasminogen activator affect its enzymatic function and fibrin specificity.

January 1, 1992Protein Engineering Design and SelectionOpen Access

Involvement of residues 296–299 in the enzymatic activity of tissue-type plasminogen activator

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Authors

NPNicholas F. PaoniUniversity of Notre Dame CRCanio J. RefinoRoche (Switzerland)KBKevin BradyRoche (Switzerland)

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Implication

Experimental analysis reveals that amino acid substitutions modify enzyme activity in tissue-type plasminogen activator, suggesting enhanced specificity.

Key Points

This research investigates how specific amino acid residues in tissue-type plasminogen activator affect its enzymatic function and fibrin specificity.
Constructed various amino acid substitution variants at positions 296-299
Evaluated enzymatic activities under different conditions
Compared activities of wild-type t-PA and KHRR 296-299 AAAA variant
Nearly all point mutants exhibited a phenotype akin to KHRR 296-299 AAAA
Multiple substitutions significantly enhanced enzymatic function compared to wild-type
KHRR 296-299 AAAA t-PA required four times more concentration to consume 50% of fibrinogen in human plasma than wild-type t-PA.

Cite This Study

Paoni et al. (1992) studied this question.

synapsesocial.com/papers/6a62c6cefe5b6bd6fe96c95b https://doi.org/10.1093/protein/5.3.259

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Implication

Experimental analysis reveals that amino acid substitutions modify enzyme activity in tissue-type plasminogen activator, suggesting enhanced specificity.

Involvement of residues 296–299 in the enzymatic activity of tissue-type plasminogen activator

Discussion

Member takes

Implication

Key Points

Cite This Study

Involvement of residues 296–299 in the enzymatic activity of tissue-type plasminogen activator

Discussion

Member takes

Implication

Key Points

Cite This Study

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