3.4.21.B2: granzyme M
This is an abbreviated version!
For detailed information about granzyme M, go to the full flat file.
Word Map on EC 3.4.21.B2
-
3.4.21.B2
-
lymphocyte
-
granule
-
killer
-
perforin
-
medicine
-
cell-mediated
-
virus-infected
-
cytolysis
-
pore-forming
-
caspase-independent
-
thiobenzyl
-
serpins
-
perforin-dependent
-
m-mediated
-
norleucine
-
noncytotoxic
- 3.4.21.B2
- lymphocyte
- granule
-
killer
- perforin
- medicine
-
cell-mediated
-
virus-infected
-
cytolysis
-
pore-forming
-
caspase-independent
-
thiobenzyl
- serpins
-
perforin-dependent
-
m-mediated
- norleucine
-
noncytotoxic
Reaction
endopeptidase activity. Cleaves substrates containing a methionine side chain at P1 =
Synonyms
Granzyme M, GrM, GrzM, Gzm M, GZmM, hGzmM, hMet-1, Met-ase-1, S01.139
ECTree
3.4.21.B2 granzyme MAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 3.4.21.B2 - granzyme M
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
acetyl-GRLL-7-amido-4-methylcoumarin + H2O
acetyl-GRLL + 7-amino-4-methylcoumarin
-
-
-
-
?
acetyl-KEPL-7-amido-4-methylcoumarin + H2O
acetyl-KEPL + 7-amino-4-methylcoumarin
-
-
-
-
?
acetyl-KEPM-7-amido-4-methylcoumarin + H2O
acetyl-KEPM + 7-amino-4-methylcoumarin
-
-
-
-
?
acetyl-KVAM-7-amido-4-methylcoumarin + H2O
acetyl-KVAM + 7-amino-4-methylcoumarin
-
-
-
-
?
acetyl-KVPL-7-amido-4-methylcoumarin + H2O
acetyl-KVPL + 7-amino-4-methylcoumarin
-
-
-
-
?
acetyl-KVPM-7-amido-4-methylcoumarin + H2O
acetyl-KVPM + 7-amino-4-methylcoumarin
-
-
-
-
?
acetyl-KYAL-7-amido-4-methylcoumarin + H2O
acetyl-KYAL + 7-amino-4-methylcoumarin
-
-
-
-
?
acetyl-KYPL-7-amido-4-methylcoumarin + H2O
acetyl-KYPL + 7-amino-4-methylcoumarin
-
-
-
-
?
acetyl-KYPM-7-amido-4-methylcoumarin + H2O
acetyl-KYPM + 7-amino-4-methylcoumarin
-
-
-
-
?
acetyl-MEPL-7-amido-4-methylcoumarin + H2O
acetyl-MEPL + 7-amino-4-methylcoumarin
-
-
-
-
?
acetyl-RYPL-7-amido-4-methylcoumarin + H2O
acetyl-RYPL + 7-amino-4-methylcoumarin
-
-
-
-
?
acetyl-VPL-7-amido-4-methylcoumarin + H2O
acetyl-VPL + 7-amino-4-methylcoumarin
-
-
-
-
?
ezrin + H2O
?
granzyme M directly and efficiently cleaves the actin-plasma membrane linker ezrin
-
-
?
heterogeneous nuclear ribonucleoprotein K + H2O
?
-
granzyme M most efficiently cleaves heterogeneous nuclear ribonucleoprotein K in the presence of RNA at multiple sites, thereby likely destroying heterogeneous nuclear ribonucleoprotein K function
-
?
N-benzyloxycarbonyl-alanyl-alanyl-methionine-thiobenzylester + H2O
N-benzyloxycarbonyl-alanyl-alanyl-methionine + phenylmethanethiol
-
-
-
?
N-benzyloxycarbonyl-alanyl-alanyl-prolyl-methionine-thiobenzylester + H2O
N-benzyloxycarbonyl-alanyl-alanyl-prolyl-methionine + phenylmethanethiol
-
-
-
?
N-benzyloxycarbonyl-alanyl-aspartyl-methionine-thiobenzylester + H2O
-benzyloxycarbonyl-alanyl-aspartyl-methionine + phenylmethanethiol
-
-
-
?
N-benzyloxycarbonyl-alanyl-lysyl-methionine-thiobenzylester + H2O
N-benzyloxycarbonyl-alanyl-lysyl-methionine + phenylmethanethiol
-
-
-
?
N-benzyloxycarbonyl-alanyl-prolyl-methionine-thiobenzylester + H2O
N-benzyloxycarbonyl-alanyl-prolyl-methionine + phenylmethanethiol
-
-
-
?
N-benzyloxycarbonyl-alanyl-seryl-methionine-thiobenzylester + H2O
N-benzyloxycarbonyl-alanyl-seryl-methionine + phenylmethanethiol
-
-
-
?
N-benzyloxycarbonyl-aspartyl-prolyl-methionine-thiobenzylester + H2O
N-benzyloxycarbonyl-aspartyl-prolyl-methionine + phenylmethanethiol
-
-
-
?
N-benzyloxycarbonyl-lysyl-prolyl-methionine-thiobenzylester + H2O
N-benzyloxycarbonyl-lysyl-prolyl-methionine + phenylmethanethiol
-
-
-
?
N-benzyloxycarbonyl-prolyl-prolyl-methionine-thiobenzylester + H2O
N-benzyloxycarbonyl-prolyl-prolyl-methionine + phenylmethanethiol
-
-
-
?
N-benzyloxycarbonyl-seryl-prolyl-methionine-thiobenzylester + H2O
N-benzyloxycarbonyl-seryl-prolyl-methionine + phenylmethanethiol
-
-
-
?
N-tert-butoxycarbonyl-Ala-Ala-Met thiobenzyl ester + H2O
N-tert-butoxycarbonyl-Ala-Ala-Met + phenylmethanethiol
-
activity only occurs with deletion mutants, but not with wild-type enzyme
-
?
N-tert-butoxycarbonyl-Ala-Ala-Met-thiobenzyl ester + H2O
N-tert-butoxycarbonyl-Ala-Ala-Met + phenylmethanethiol
-
cleaves thiobenzylester substrates specifically after methionine, norleucine or leucine residues in the primary substrate site P1
-
?
N2-Cbz-L-Asp(O-tBut)-L-Pro-L-Met thiobenzyl ester + H2O
N2-Cbz-L-Asp(O-tBut)-L-Pro-L-Met + phenylmethanethiol
-
-
-
?
N2-CBZ-O3-tBut-L-Ser-L-Pro-L-Met-SBzl + H2O
N2-CBZ-O3-tBut-L-Ser-L-Pro-L-Met + phenylmethanethiol
-
-
-
?
N2-[(benzyloxy)carbonyl]-N6-(tert-butoxycarbonyl)-L-lysyl-L-prolyl-L-methionyl thiobenzyl ester + H2O
N2-[(benzyloxy)carbonyl]-N6-(tert-butoxycarbonyl)-L-lysyl-L-prolyl-L-methionine + phenylmethanethiol
-
-
-
?
proteinase inhibitor 9 + H2O
?
-
effective hydrolysis and inactivation, bypassing proteinase inhibitor 9 inhibition of granzyme B
-
-
?
survivin + H2O
?
the inhibitor of the apoptosis gene family member survivin is a physiological substrate for GzmM. GzmM hydrolyzes survivin at Leu-138 to remove the last four C-terminal residues. The truncated form is more rapidly hydrolyzed through proteasome-mediated degradation
-
-
?
topoisomerase II alpha + H2O
?
-
cleavage of topoisomerase II alpha by granzyme M at Leu1280 separates topoisomerase II alpha functional domains from the nuclear localization signals and leads to nuclear exit of topoisomerase II alpha catalytic activity
-
?
alpha-tubulin + H2O
?
direct alpha-tubulin proteolysis by granzyme M is complex and occurs at multiple cleavage sites, one of them being Leu at position 269. Granzyme M disturbs tubulin polymerization dynamics in vitro and induces microtubule network disorganization in tumor cells in vivo
-
-
?
alpha-tubulin + H2O
?
direct alpha-tubulin proteolysis by granzyme M is complex and occurs at multiple cleavage sites, one of them being Leu at position 269. Granzyme M disturbed tubulin polymerization dynamics in vitro and induced microtubule network disorganization in tumor cells in vivo
-
-
?
human Fas-associated protein with Death Domain + H2O
?
-
cleavage at residue Met196
-
?
human Fas-associated protein with Death Domain + H2O
?
-
cleavage at residue Met196
-
?
inhibitor of caspase-activated DNase + H2O
?
-
direct degradation to release the nuclease activity of caspase-activated DNase for damaging DNA
-
-
?
mouse Fas-associated protein with Death Domain mutant V193M/L194S + H2O
?
no substrate: wild-type mouse Fas-associated protein with Death Domain lacking a residue corresponding to Met196 of the human substrate
cleavage at residue M193
-
?
mouse Fas-associated protein with Death Domain mutant V193M/L194S + H2O
?
no substrate: wild-type mouse Fas-associated protein with Death Domain lacking a residue corresponding to Met196 of the human substrate
cleavage at residue M193
-
?
nucleophosmin + H2O
?
the nucleolar phosphoprotein, nucleophosmin (NPM), is cleaved and inactivated. Targeting of NPM by granzyme M may contribute to tumor cell eradication by abolishing NPM function
-
-
?
nucleophosmin + H2O
?
the nucleolar phosphoprotein, nucleophosmin (NPM), is cleaved and inactivated
-
-
?
poly(ADP-ribose) polymerase + H2O
?
-
cleavage to prevent cellular DNA repair and force apoptosis
-
-
?
additional information
?
-
-
cleaves the carboxyl side of long narrow hydrophobic amino acids, such as methionine, but not large, bulky hydrophobic amino acids such as phenylalanine
-
?
additional information
?
-
-
hydrolyzes substrates containing a methionine-side chain at P1
-
?
additional information
?
-
-
participates in target cell death inflicted by cytotoxic lymphocytes
-
?
additional information
?
-
-
involved in granule exocytosis form of target cell death induced by cytotoxic lymphocytes
-
?
additional information
?
-
-
preference of proline over alanine at P2 and leucine over norleucine over methionine at P1, broad specificity at P3 and P4
-
-
?
additional information
?
-
the enzyme has a strong preference for Pro at the P2 position and Ala, Ser, or Asp at the P3 position
-
-
?
additional information
?
-
-
the enzyme has a strong preference for Pro at the P2 position and Ala, Ser, or Asp at the P3 position
-
-
?
additional information
?
-
isolated granzyme M induces cell death and disorganizes the microtubule network by targeting alpha-tubulin. Granzyme M inactivates the GzmB inhibitor protease inhibitor 9, thereby increasing the susceptibility of target cells to granzyme B-induced apoptosis
-
-
?
additional information
?
-
the recombinant GrM protein displays proteolytic activity only against a synthetic substrate that matches with the known cleavage specificity of the granzyme, which is after a Leu
-
-
?
additional information
?
-
-
the recombinant GrM protein displays proteolytic activity only against a synthetic substrate that matches with the known cleavage specificity of the granzyme, which is after a Leu
-
-
?
