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3.4.22.B69: falcipain-2

This is an abbreviated version!
For detailed information about falcipain-2, go to the full flat file.

Word Map on EC 3.4.22.B69

Reaction

The enzyme plays a key role in the hydrolysis of hemoglobin by the parasite Plasmodium falciparum. Preferred cleavage sites display arginine in P1, leucine in P2, and phenylalanine in P1' =

Synonyms

falcipain 2, falcipain-2, FP-2, Fp2, haemoglobinase

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.22 Cysteine endopeptidases
                3.4.22.B69 falcipain-2

Substrates Products

Substrates Products on EC 3.4.22.B69 - falcipain-2

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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Abz-KLRFSKQ-EDDnp + H2O
?
show the reaction diagram
-
-
-
-
?
Abz-KLRSSKQ-EDDnp + H2O
?
show the reaction diagram
-
-
-
-
?
Abz-KLRSXKQ-EDDnp + H2O
Abz-KLRS + XKQ-EDDnp
show the reaction diagram
-
-
-
-
?
Abz-KLRXSKQ-EDDnp + H2O
Abz-KLR + XSKQ-EDDnp
show the reaction diagram
-
-
-
-
?
Abz-KLXSSKQ-EDDnp + H2O
Abz-KLX + SSKQ-EDDnp
show the reaction diagram
-
-
-
-
?
Abz-KXRSSKQ-EDDnp + H2O
Abz-KXR + SSKQ-EDDnp
show the reaction diagram
-
-
-
-
?
Abz-MISLMKRPPGFSPFRSSRI-NH2 + H2O
?
show the reaction diagram
-
the peptide corresponds to the Met375 to Ile393 sequence of high molecular weight kininogen. The enzyme preferentially accommodates at the S1 subsite the positively charged residue Arg, followed by Gln. At the P2 position, the enzyme shows a clear preference for the hydrophobic aliphatic residue Leu over Phe. The subsite S3 of FP-2 shows a broad specificity with slight preference of Lys in the P3 position
the generated fragments are KRPPGFSPFR (Lys-bradykinin, 63%), RPPGFSPFR (bradykinin, 30%), and MKRPPGFSPFR (Met-Lys-bradykinin, 7%)
-
?
Abz-XLRSSKQ-EDDnp + H2O
Abz-XLR + SSKQ-EDDnp
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Leu-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Leu-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
Cbz-Phe-Arg-7-amido-4-methylcoumarin + H2O
Cbz-Phe-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
D-Val-Leu-Arg-7-amido-4-methylcoumarin + H2O
D-Val-Leu-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
Hemoglobin + H2O
?
show the reaction diagram
high molecular weight kininogen + H2O
Met-Lys-bradykinin + Lys-bradykinin + bradykinin + ?
show the reaction diagram
-
-
-
-
?
N-benzyloxycarbonyl-Leu-Arg 7-amido-4-methylcoumarin + H2O
N-benzyloxycarbonyl-Leu-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
VLK-4-nitroanilide + H2O
VLK + 4-nitronaniline
show the reaction diagram
-
-
-
?
Z-Leu-Arg-7-amido-4-methylcoumarin + H2O
Z-Leu-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
Z-Phe-Arg-7-amido-4-methylcoumarin + H2O
Z-Phe-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
the falcipain-2 prodomain efficiently inhibits falcipain-2, falcipain-2', berghepain-2, falcipain-3, cathepsin K, cathepsin L, cathepsin B, and cruzain, but it does not inhibit cathepsin C, pepsin, alpha-chymotrypsin, and collagenase
-
-
?