Literature summary for 3.4.24.51 extracted from

  • Guo, X.; Zeng, L.; Lee, W.; Zhang, Y.; Jin, Y.
    Isolation and cloning of a metalloproteinase from king cobra snake venom (2007), Toxicon, 49, 954-965.
    View publication on PubMed
Search for more literature for 3.4.24.51

Cloned(Commentary)

Cloned (Comment) Organism
DNA and amino acid sequence determination and analysis, phylogenetic tree Ophiophagus hannah

Inhibitors

Inhibitors Comment Organism Structure
EDTA complete inhibition Ophiophagus hannah
additional information no inhibition by PMSF Ophiophagus hannah

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
 Ophiophagus hannah
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
additional information metalloproteinase Ophiophagus hannah

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
50000
-
 1 * 50000, SDS-PAGE, 1 * 47344, sequence calculation Ophiophagus hannah
55000
-
 gel filtration Ophiophagus hannah
47344
-
 1 * 50000, SDS-PAGE, 1 * 47344, sequence calculation Ophiophagus hannah

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Ophiophagus hannah the enzyme inhibits platelet aggregation induced by ADP, TMVA, and stejnulxin ?
-
 ?
Fibrinogen + H2O Ophiophagus hannah human substrate, specific degradation of the alpha-chain, no activity with beta-chain and gamma-chain, the enzyme has a fibrinogenolytic activity and hemorrhagic activity in mice, overview ?
-
 ?

Organism

Organism UniProt Comment Textmining
Ophiophagus hannah A3R0T9 king cobra
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein ohagin contains four potential N-glycosylation sites Ophiophagus hannah

Purification (Commentary)

Purification (Comment) Organism
native enzyme by gel filtration, ion exchange and heparin affinity chromatography Ophiophagus hannah

Source Tissue

Source Tissue Comment Organism Textmining
venom
-
 Ophiophagus hannah
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
 hemorrhagic activity in mice, overview Ophiophagus hannah

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the enzyme inhibits platelet aggregation induced by ADP, TMVA, and stejnulxin Ophiophagus hannah ?
-
 ?
Fibrinogen + H2O human substrate, specific degradation of the alpha-chain, no activity with beta-chain and gamma-chain, the enzyme has a fibrinogenolytic activity and hemorrhagic activity in mice, overview Ophiophagus hannah ?
-
 ?
Fibrinogen + H2O specific degradation of the alpha-chain of the human substrate, while the beta- and gamma-chains are not hydrolyzed Ophiophagus hannah ?
-
 ?

Subunits

Subunits Comment Organism
monomer 1 * 50000, SDS-PAGE, 1 * 47344, sequence calculation Ophiophagus hannah
More MALDI-TOF enzyme peptide mass fingerprinting, the enzyme contains a signal peptide, a proprotein, and a metalloproteinase, a disintegrin-like, and a cysteine-rich domain, overview Ophiophagus hannah

Synonyms

Synonyms Comment Organism
ohagin
-
 Ophiophagus hannah

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Ophiophagus hannah

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.6
-
 assay at Ophiophagus hannah

pI Value

Organism Comment pI Value Maximum pI Value
Ophiophagus hannah sequence calculation
-
 5.84