Dataset Information

Lee2010_ThrombinActivation_OneForm_reduced

ABSTRACT: Chang Jun Lee, Sangwook Wu, Changsun Eun & Lee G. Pedersen. A revisit to the one form kinetic model of prothrombinase. Biophysical Chemistry 149, 1-2 (2010).

Thrombin is generated enzymatically from prothrombin by two pathways with the intermediates of meizothrombin and prethrombin-2. Experimental concentration profiles from two independent groups for these two pathways have been re-analyzed. By rationally combining the independent data sets, a simple mechanism can be established and rate constants determined. A structural model is consistent with the data-derived finding that mechanisms that feature channeling or ratcheting are not necessary to describe thrombin production.

ORGANISM(S): Eukaryota

SUBMITTER: Lucian Smith

PROVIDER: MODEL1108260003 | biostudies-other |

SECONDARY ACCESSION(S): 20435402

REPOSITORIES: biostudies-other

ACCESS DATA

Publications

Further evidence for two functional forms of prothrombinase each specific for either of the two prothrombin activation cleavages.

Kim Paul Y PY Nesheim Michael E ME

The Journal of biological chemistry 20070828 45

Previous work showed that prothrombin derivatives cleavable only at Arg-320 (rMZ) or Arg-271 (rP2) are partial, rather than competitive, inhibitors of prothrombin activation by prothrombinase. A "ping-pong"-like model, which posits two equilibrating forms of prothrombinase, explained the inhibition pattern. The present studies were undertaken to further investigate this putative mechanism. Two models were developed, one allowing for one form of the enzyme and the other allowing for two forms. Bo ...[more]

PMID: 17726029

Publication: 1/2

Dataset Information

Lee2010_ThrombinActivation_OneForm_reduced

Publications

Further evidence for two functional forms of prothrombinase each specific for either of the two prothrombin activation cleavages.

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