Information on EC 3.4.24.51 - ophiolysin

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


The expected taxonomic range for this enzyme is: Ophiophagus hannah

EC NUMBER
COMMENTARY hide
3.4.24.51
-
RECOMMENDED NAME
GeneOntology No.
ophiolysin
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Cleavage of Asn3-/-Gln, Gln4-/-His, His10-/-Leu, Ala14-/-Leu, and Tyr16-/-Leu in insulin B chain
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
-
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
casein + H2O
?
show the reaction diagram
-
-
-
-
?
Fibrinogen + H2O
?
show the reaction diagram
insulin B chain + H2O
Phe-Val-Asn + Gln + HLCGSH + LVEA + Leu-Tyr + LVCGERGFFYTPKA
show the reaction diagram
-
-
-
-
?
Insulin B-chain + H2O
Hydrolyzed insulin B-chain
show the reaction diagram
-
cleavage of Asn3-Gln, Gln4-His, His10-Leu, Ala14-Leu and Tyr16-Leu
-
-
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
Fibrinogen + H2O
?
show the reaction diagram
A3R0T9
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
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cysteine
-
strongly inhibits
formaldehyde
-
-
additional information
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.2
-
assay at
additional information
-
basic enzyme
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.84
sequence calculation
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
47344
1 * 50000, SDS-PAGE, 1 * 47344, sequence calculation
50000
1 * 50000, SDS-PAGE, 1 * 47344, sequence calculation
55000
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
ohagin contains four potential N-glycosylation sites
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
by successive chromatographies
-
native enzyme by gel filtration, ion exchange and heparin affinity chromatography
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, phylogenetic tree