Any feedback?
Please rate this page
(all_enzymes.php)
(0/150)

BRENDA support

3.4.22.62: caspase-9

This is an abbreviated version!
For detailed information about caspase-9, go to the full flat file.

Word Map on EC 3.4.22.62

Reaction

strict requirement for an Asp residue at position P1 and with a marked preference for His at position P2. It has a preferred cleavage sequence of Leu-Gly-His-Asp-/-Xaa =

Synonyms

APAF, Apaf-3, apoptotic protease activating factor 3, apoptotic protease Mch-6, C14.010, CASP-9, casp9, casp9-gamma, caspase 9, caspase-9, ICE-LAP6, ICE-like apoptotic protease 6, Mch6

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.22 Cysteine endopeptidases
                3.4.22.62 caspase-9

Engineering

Engineering on EC 3.4.22.62 - caspase-9

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
-
optical sensor for the detection of caspase-9 in a single cell. LEHD-7-amido-4-methylcoumarin covalently attached on the nanoprobe tip of the optical sensor is cleaved during apoptosis by caspase-9 generating free 7-amino-4-methylcoumarin
C172A
-
the mutant enzyme shows reduced zinc binding compared to the wild-type enzyme
C239S
-
the mutant enzyme shows reduced zinc binding compared to the wild-type enzyme
C272A
-
the mutant enzyme shows reduced zinc binding compared to the wild-type enzyme
C272A/C287A
-
the mutant enzyme shows highly reduced zinc binding compared to the wild-type enzyme
C287A
C287A/C239S
-
the mutant enzyme shows reduced zinc binding compared to the wild-type enzyme
C403S
point mutation at C403 of caspase-9 impairs its activation mediated by H2O2, interaction with APAF-1 diminished through the abolition of disulfide formation, weaker association between cytochrome c and the C403S mutant than that between cytochrome c and wild-type caspase-9
DELTA1-111
-
a truncated form of procaspase-9 missing the first 111 amino acids, and a variety of mutants derived therefrom are expressed in Echerichia coli inclusion bodies. Upon refolding to active enzyme, DELTA1-111 procaspase-9 and mutants are recovered at purity greater than 95% with a final yield of 20-35 mg/L cell culture. the active procaspaseretains its prosegment, while undergoing major auto processing at ASp315 and a minor cleavage at Glu306
DELTA1-111/DELTAA316-D330
DELTA1-111/E306A/D315A
-
E306A/D315A mutation blocks autoprocessing and shifts pH optimum from pH 6.2 for DELTA1-111 to pH 7.2. Activity with acetyl-LEHD-7-amido-4-trifluoromethyl coumarin is identical to the activity of mutant DELTA1-111
DELTA1-111/E306D/D315A
DELTA1-111/E306D/DELTAA316-D330
H237A
-
the active site mutant enzyme shows reduced zinc binding compared to the wild-type enzyme
T125A/C287A
site-directed mutagenesis, immunofluorescence staining of cells transiently transfected with vectors encoding caspase-9 double mutant
C299G
-
site-directed mutagenesis, the mutant displays significantly decreased proteolytic activity compared to the wild-type enzyme
H249D
-
site-directed mutagenesis, the mutant displays significantly decreased proteolytic activity compared to the wild-type enzyme
L228V
-
site-directed mutagenesis
S348A
introduction of point mutants into full-length murine caspase-9 (mC-9) cDNA, generated by a two-step PCR method, efficiently cleaved by the active initiator caspase
S348G
introduction of point mutants into full-length murine caspase-9 (mC-9) cDNA, generated by a two-step PCR method, efficiently cleaved by the active initiator caspase
S348V
introduction of point mutants into full-length murine caspase-9 (mC-9) cDNA, generated by a two-step PCR method, efficiently cleaved by the active initiator caspase
S350A
introduction of point mutants into full-length murine caspase-9 (mC-9) cDNA, generated by a two-step PCR method, efficiently cleaved by the active initiator caspase
additional information