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enzymatic reaction
A chemical reaction catalyzed by an enzyme. An enzymatic reaction consists of substrate(s), enzyme & product(s). The enzyme is unchanged by the reaction.
Properties
GENERAL: catalytic reaction
SPECIFIC: biochemical ligation
sialylation
active transport
protein phosphorylation
proteolytic cleavage
template-directed reaction
ENZYME: plasmin
COMPARTMENT: plasma
MOTIF: charge relay system
MOTIF: aspartate residue
histidine residue
serine residue
kringle domain
allosteric site
FOR-BINDING-OF: complement C1 inhibitor
STATE: active state
SUBSTRATE: coagulation factor V
COMPARTMENT: plasma
MOTIF: signal sequence {1-28}
F5/8 type A 1 {30-329}
MOTIF: Plastocyanin-like 1 {30-193}
N-glycosylation site {N51}
N-glycosylation site {N55}
Ca+2-binding site
SITE: 139-139
Ca+2-binding site
SITE: 140-140
cysteine residue {C167}
MODIFICATION: cysteine residue {C193}
cysteine residue {C193}
MODIFICATION: cysteine residue {C167}
Plastocyanin-like 2 {203-329}
N-glycosylation site {N239}
cysteine residue {C248}
MODIFICATION: cysteine residue {C329}
N-glycosylation site {N297}
cysteine residue {C329}
MODIFICATION: cysteine residue {C248}
proteolytic site {334-335}
F5/8 type A 2 {348-684}
MOTIF: Plastocyanin-like 3 {348-526}
N-glycosylation site {N382}
N-glycosylation site {N460}
N-glycosylation site {N468}
cysteine residue {C500}
MODIFICATION: cysteine residue {C526}
cysteine residue {C526}
MODIFICATION: cysteine residue {C500}
proteolytic site {534-535}
Plastocyanin-like 4 {536-684}
N-glycosylation site {N554}
cysteine residue {C603}
MODIFICATION: cysteine residue {C684}
Thr phosphorylation site {T640}
cysteine residue {C684}
MODIFICATION: cysteine residue {C603}
B {692-1573}
MOTIF: proteolytic site {707-708}
proteolytic site {737-738}
N-glycosylation site {N741}
N-glycosylation site {N752}
N-glycosylation site {N760}
N-glycosylation site {N776}
N-glycosylation site {N782}
N-glycosylation site {N821}
domain {895-928}
1-1 {895-911}
1-2 {912-928}
N-glycosylation site {N938}
N-glycosylation site {N977}
proteolytic site {1022-1023}
proteolytic site {1046-1047}
N-glycosylation site {N1074}
N-glycosylation site {N1083}
N-glycosylation site {N1103}
N-glycosylation site {N1106}
Ser phosphorylation site {S1150}
domain {1185-1501}
consensus repeat {1185-1501} (35)
N-glycosylation site {N1499}
N-glycosylation site {N1559}
proteolytic site {1573-1574}
F5/8 type A 3 {1578-1907}
MOTIF: Plastocyanin-like 5 {1578-1751}
N-glycosylation site {N1703}
cysteine residue {C1725}
MODIFICATION: cysteine residue {C1751}
cysteine residue {C1751}
MODIFICATION: cysteine residue {C1725}
Plastocyanin-like 6 {1761-1907}
copper [Cu]-binding site
SITE: 1843-1843
MOTIF: histidine residue (3)
copper [Cu]-binding site
SITE: 1845-1845
MOTIF: histidine residue (3)
coagulation factors 5/8 type C domain (FA58C) {1907-2061}
MOTIF: cysteine residue {C1907}
MODIFICATION: cysteine residue {C2061}
N-glycosylation site {N2010}
cysteine residue {C2061}
MODIFICATION: cysteine residue {C1907}
coagulation factors 5/8 type C domain (FA58C) {2066-2221}
MOTIF: cysteine residue {C2066}
MODIFICATION: cysteine residue {C2221}
N-glycosylation site {N2209}
cysteine residue {C2221}
MODIFICATION: cysteine residue {C2066}
PRECURSOR-FOR: coagulation factor Va
PRODUCT: peptide
References
Fibrinolysis, Thrombosis, & Hemostasis: Concepts,
Perspectives, and Clinical Applications. S Sherry,
Lea & Febiger, Philadelphia, 1992, pg 81