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Literature summary extracted from

  • Kazemali, M.; Majidzadeh-A, K.; Sardari, S.; Saadatirad, A.H.; Khalaj, V.; Zarei, N.; Barkhordari, F.; Adeli, A.; Mahboudi, F.
    Design of a novel chimeric tissue plasminogen activator with favorable Vampire bat plasminogen activator properties (2014), Enzyme Microb. Technol., 67, 82-86.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.4.21.68 Fibrin activates the wild-type enzyme, and also the chimeric mutant enzyme, the latter to an extremely higher degree, overview Homo sapiens

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.4.21.68 recobinant expression of wild-type and mutant enzymes in Pichia pastoris strain GS115, cloning in Escherichia coli strain Top10F Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
3.4.21.68 K213A/H214A/R215A/R216A construction of a chimeric tissue plasminogen activator (t-PA) through kringle 2 domain removal and replacement of t-PA finger domain with the Vampire bat plasminogen activator one. Vampire bat plasminogen activator (b-PA) is a plasminogen activator with higher fibrin affinity and specificity in comparison to t-PA resulting in reduced probability of hemorrhage. b-PA is also resistant to plasminogen activator inhibitor-1 showing higher half-life compared to other variants of t-PA. The KHRR sequence at the initial part of protease domain is replaced by four alanine residues. The activity of therecombinant protein in the presence of fibrin is 1560 times more than its activity in the absence of fibrin, showing its higher specificity to fibrin. The chimeric enzyme shows 1.2fold higher fibrin binding in comparison to full-length enzyme Homo sapiens

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.21.68 plasminogen activator inhibitor-1 PAI-1, the recombinant chimeric t-PA/b-PA mutant enzyme is 44% less sensitive compared to wild-type tissue plasminogen activator, t-PA Homo sapiens

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.4.21.68 70000
-
 x * 75000, recombinant chimeric enzyme mutant, SDS-PAGE, x * 70000, wild-type t-PA, SDS-PAGE, the wild-type enzyme holds five domains including finger, epidermal growth factor, kringle 1, kringle 2 and protease Homo sapiens
3.4.21.68 75000
-
 x * 75000, recombinant chimeric enzyme mutant, SDS-PAGE, x * 70000, wild-type t-PA, SDS-PAGE, the wild-type enzyme holds five domains including finger, epidermal growth factor, kringle 1, kringle 2 and protease Homo sapiens

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.4.21.68 plasminogen + H2O Homo sapiens activation plasmin + ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.4.21.68 Homo sapiens P00750
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.21.68 plasminogen + H2O activation Homo sapiens plasmin + ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.4.21.68 ? x * 75000, recombinant chimeric enzyme mutant, SDS-PAGE, x * 70000, wild-type t-PA, SDS-PAGE, the wild-type enzyme holds five domains including finger, epidermal growth factor, kringle 1, kringle 2 and protease Homo sapiens

Synonyms

EC Number Synonyms Comment Organism
3.4.21.68 Alteplase
-
 Homo sapiens
3.4.21.68 t-PA
-
 Homo sapiens

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.4.21.68 37
-
 assay at Homo sapiens

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.4.21.68 7.4
-
 assay at Homo sapiens