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3.4.21.38: coagulation factor XIIa

This is an abbreviated version!
For detailed information about coagulation factor XIIa, go to the full flat file.

Word Map on EC 3.4.21.38

Reaction

selective cleavage of Arg-/-Ile bonds in factor VII to form factor VIIa and factor XI to form factor XIa =

Synonyms

activated coagulation factor XII, activated factor XII, alpha-FXIIa, alphaFXIIa, beta-factor XIIa, beta-FXIIa, blood coagulation factor XII, blood-coagulation factor XII, activated beta, blood-coagulation factor XIIabeta, blood-coagulation factor XIIf, coagulation beta-factor XIIa, coagulation factor XII, coagulation factor XIIa, F12, factor XII, factor XII Osaka, factor XIIa, FXII, FXIIa, HAF, Hageman factor, Hageman factor beta-fragment, Hageman factor fragment HFf, Hagemann factor, kallikreinogen, activator, prealbumin activator, prekallikrein activator, single-chain FXII

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.21 Serine endopeptidases
                3.4.21.38 coagulation factor XIIa

Engineering

Engineering on EC 3.4.21.38 - coagulation factor XIIa

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A324P/G531E
-
naturally occuring mutation, reduced activity of prekallikrein cleavage
C135X
naturally occuring mutation, Korean patient 2
G582S
mutation of c11744G>A plus insertion mutation c1093_1094insC, pK365QfsX69, naturally occuring mutation, Korean patient 3
K346N
-
the mutation, a G to C point mutation at nucleotide 9845, causes a replacement in the catalytic domain, and congenital FXII deficiency as a rare coagulation disease and an autosomal recessive trait, designated as factor XII Ofunato. The mutant shows a lower level of accumulation in the cells and reduced secretion in culture medium.compared to the wild-type. The mutant shows unaltered FXII mRNA levels but increased degenration of the mutant mRNA in the pre-Golgi compartment of transfected CHO-K1 cells involving the proteasome, overview
P547L
-
the mutation is associated with factor XII deficiency
Q501T
-
the mutation is associated with factor XII deficiency
R334A/R343A/R353A
-
the mutant lacks the Arg334, Arg343, and Arg353 cleavage sites required for conversion to the enzyme form betaFXIIa and shows proteolytic activity that is about 3000fold weaker than that of the wild type enzyme
R334A/R344A/R353A
-
in the presence of polyphosphate, the mutant converts factor XII to its active form alpha-fXIIa, and also converts factor XI to its active form fXIa. The mutant does not undergo autocatalysis to alpha-fXIIa in the presence of polyphosphate, and is resistant to cleavage by alpha-kallikrein and factor XIIa
R353A
-
the mutant lacks the Arg353 cleavage site required for conversion to the activated enzyme form alphaFXIIa and shows proteolytic activity that is several orders of magnitude weaker than that of the wild type enzyme
S528T/G582S
naturally occuring mutation, Korean patient 1
S544A
-
active site mutant
S554A
-
inactive
T309K
-
naturally occuring mutation of factor XII, isolated from hereditary angioedema patients. The mutation does not affect FXII surface activation or kallikrein-like activity, and does not lead to a gain-of-function of FXIIa, overview
additional information