March 23, 1976Biochemistry

Specificity of thrombin: evidence for selectivity in acylation rather than binding for p-nitrophenyl α-amino-p-toluate

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Population

Enzymes (thrombin, trypsin, and plasmin) reacting with synthesized ester analogues

Comparison

p-nitrophenyl alpha-amino-p-toluate hydrobromide vs p-nitrophenyl p-guanidinobenzoate hydrochloride…

Design

Preclinical

Authors

TRThomas J. RyanColumbia University Irving Medical Center JFJohn W. FentonUniversity of Portsmouth TCTien-Ling ChangNew York University

Discussion

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Implication

Acylation barriers, not binding, drive thrombin's arginyl preference; extends enzyme kinetics but leaves open physiologic or therapeutic translation.

Structured PICO

Population

Enzymes (thrombin, trypsin, and plasmin) reacting with synthesized ester analogues

Intervention

p-nitrophenyl alpha-amino-p-toluate hydrobromide (lysyl ester analogue)

Comparator

p-nitrophenyl p-guanidinobenzoate hydrochloride (arginyl ester analogue) and comparison across enzymes

Outcome

Kinetic parameters: Ks (enzyme-substrate binding), k2 (acylation), and k3 (deacylation)surrogate

Thrombin's specificity and limited cleavage of lysyl bonds are driven by restricted acylation rather than substrate binding, highlighting a stringent spatial requirement in its active site.

Cite This Study

Ryan et al. (1976) studied this question.

synapsesocial.com/papers/6a80bb2604b22a52ede4ac1f https://doi.org/10.1021/bi00651a026

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Implication

Acylation barriers, not binding, drive thrombin's arginyl preference; extends enzyme kinetics but leaves open physiologic or therapeutic translation.

Specificity of thrombin: evidence for selectivity in acylation rather than binding for p-nitrophenyl α-amino-p-toluate

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Specificity of thrombin: evidence for selectivity in acylation rather than binding for p-nitrophenyl α-amino-p-toluate

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Also Consider

Also Consider