Any feedback?
Literature summary for 3.4.21.7 extracted from
- The plasmin-antiplasmin system: structural and functional aspects (2011), Cell. Mol. Life Sci., 68, 785-801.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| additional information | the main physiological activators of plasminogen are tissue-type plasminogen activator, which is mainly involved in the dissolution of the fibrin polymers by plasmin, and urokinase-type plasminogen activator, which is primarily responsible for the generation of plasmin activity in the intercellular space. Both activators are multidomain serine proteases | Homo sapiens |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| alpha2-antiplasmin | the main physiological inhibitor and a serpin | Homo sapiens | |
| alpha2-Macroglobulin | general protease inhibitor | Homo sapiens | |
| histidine-rich glycoprotein | binds at sites of tissue injury and seems to act as a high-affinity receptor to immobilize plasminogen on cell surfaces | Homo sapiens | |
| additional information | features and mode of action of plasmin inhibitors, detailed overview | Homo sapiens | |
| neuroserpin | mainly expressed in the brain, a serpin and single-chain glycoprotein of 55 kDa containing three potential N-glycosylation sites at Asn141, Asn305, and Asn385 | Homo sapiens | |
| plasminogen activator inhibitors 1 | - |
Homo sapiens | |
| plasminogen activator inhibitors 2 | - |
Homo sapiens |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| extracellular | - |
Homo sapiens | - |
- |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 88432 | - |
x * 90000, plasminogen, SDS-PAGE, x * 88432, plasminogen, sequence determination | Homo sapiens |
| 90000 | - |
x * 90000, plasminogen, SDS-PAGE, x * 88432, plasminogen, sequence determination | Homo sapiens |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| fibrin + H2O | Homo sapiens | - |
soluble fibrin fragments | - |
? |  |
| additional information | Homo sapiens | rather broad specificity of plasmin in vivo catalyzing the inactivation and degradation of matrix proteins such as collagens, fibronectin, and laminins, and components of the blood coagulation cascade such as coagulation factor FVa, von Willebrand factor, and thrombospondin | ? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | P00747 | plasminogen; gene PLG | - |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| glycoprotein | the human plasminogen is partially N-glycosylated at Asn289 and O-glycosylated at Ser249 and Thr346 giving rise to plasminogen variants I (Asn289, Thr346) and II (only Thr346) | Homo sapiens |
| phosphoprotein | plasminogen is partially phosphorylated at Ser578 | Homo sapiens |
| proteolytic modification | the main physiological activators of plasminogen are tissue-type plasminogen activator, which is mainly involved in the dissolution of the fibrin polymers by plasmin, and urokinase-type plasminogen activator, which is primarily responsible for the generation of plasmin activity in the intercellular space. Both activators are multidomain serine proteases. Pgn is activated by the two main physiological plasminogen activators to the active, two-chain plasmin molecule held together by two interchain disulfide bridges, Cys548-Cys666, Cys558-Cys566, by cleavage of the Arg561-Val562 peptide bond and the release of the 77-residue N-terminal peptide. Two N-terminally different forms of plasminogen exist, Glu-Pgn and Lys-Pgn. Lys-Pgn is formed by cleavage of the Lys77-Lys78 peptide bond in Glu-Pgn, releasing the N-terminal peptide | Homo sapiens |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| commercial preparation | - |
Homo sapiens | - |
| plasma | in blood as zymogen plasminogen | Homo sapiens | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| fibrin + H2O | - |
Homo sapiens | soluble fibrin fragments | - |
? | |
| fibrin + H2O | cleavage of the Lys583-Met584 peptide bond in the Aalpha chain, followed by the cleavage of the peptide bonds Lys206-Met207 and Lys230-Ala231, also in the Aalpha chain, thus releasing a C-terminal 40-kDa fragment and generating fragment X possessing 260 kDa. Cleavage of fragment X in all three chains results in one fragment Y (160 kDa) and one fragment D (100 kDa), and further cleavage of fragment Y produces a second fragment D and fragment E (60 kDa) | Homo sapiens | soluble fibrin fragments | - |
? | |
| additional information | rather broad specificity of plasmin in vivo catalyzing the inactivation and degradation of matrix proteins such as collagens, fibronectin, and laminins, and components of the blood coagulation cascade such as coagulation factor FVa, von Willebrand factor, and thrombospondin | Homo sapiens | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 90000, plasminogen, SDS-PAGE, x * 88432, plasminogen, sequence determination | Homo sapiens |
| More | plasminogen is a single-chain, multidomain glycoprotein, and is composed of an N-terminal peptide, five triple-loop structures stabilized by three intrachain disulfide bridges called kringles, and the trypsin-like serine protease part carrying the catalytic triad His603, Asp646, and Ser741. Primary structure of human plasminogen, overview. The three-dimensional structural model of human plasminogen based on known and overlapping 3-D structures of plasminogen fragments exhibits a spiral shape | Homo sapiens |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| More | plasminogen is a member of the peptidase S1 family | Homo sapiens |
General Information
| General Information | Comment | Organism |
|---|---|---|
| malfunction | Defects or mutations in the PLG gene are the cause of thrombophilia, a form of recurrent thrombosis, and type I plasminogen deficiency. Ligneous conjunctivitis is usually the most common and initial form of type I plasminogen deficiency and is a rare form of chronic conjunctivitis characterized by chronic tearing and redness of the conjunctivae | Homo sapiens |
| metabolism | besides the main physiological inhibitor alpha2-antiplasmin, the plasmin-antiplasmin system is also regulated by the general protease inhibitor alpha2-macroglobulin, a member of the protease inhibitor I39 family. The activity of the plasminogen activators is primarily regulated by the plasminogen activator inhibitors 1 and 2, members of the serine protease inhibitor superfamily | Homo sapiens |
| additional information | the catalytic triad is formed by His603, Asp646, and Ser741 | Homo sapiens |
| physiological function | primary function of plasmin is the cleavage of insoluble fibrin polymers at specific sites resulting in soluble fragments. In addition, plasmin acts as a proteolytic factor in many other physiological processes such as mediation of cell migration by degrading the extracellular matrix, wound healing, tissue remodelling, angiogenesis, embryogenesis, and pathogen and tumour cell invasion. The plasmin-antiplasmin system plays a key role in blood coagulation and fibrinolysis. Plasmin and alpha2-antiplasmin are primarily responsible for a controlled and regulated dissolution of the fibrin polymers into soluble fragments | Homo sapiens |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
