3.4.22.40: bleomycin hydrolase
This is an abbreviated version!
For detailed information about bleomycin hydrolase, go to the full flat file.
Word Map on EC 3.4.22.40
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3.4.22.40
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luteinizing
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paraoxonase
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thiolactone
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helveticus
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peplomycin
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lutropins
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corneocytes
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homocysteinylation
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beta-naphthylamide
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medicine
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hcy-thiolactone
- 3.4.22.40
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luteinizing
- paraoxonase
- thiolactone
- helveticus
- peplomycin
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lutropins
- corneocytes
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homocysteinylation
- beta-naphthylamide
- medicine
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hcy-thiolactone
Reaction
Inactivates bleomycin B2 (a cytotoxic glycometallopeptide) by hydrolysis of a carboxyamide bond of beta-aminoalanine, but also shows general aminopeptidase activity. The specificity varies somewhat with source, but amino acid arylamides of Met, Leu and Ala are preferred =
Synonyms
aminopeptidase C, aminopeptidase H, ApsC, BANA-hydrolase, BH, BH protein, Bleomycin hydrolase, BLH, Blh1p, BLM hydrolase, Blmh, BLMH protein, BMH, citrulline aminopeptidase, Gal6p, Hcy-thiolactonase, homocysteine thiolactonase, HTLase, hydrolase H, More, PEPC, yBLH, yeast cysteine protease
ECTree
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Substrates Products
Substrates Products on EC 3.4.22.40 - bleomycin hydrolase
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REACTION DIAGRAM
6'-deoxy bleomycin A2 + H2O
6'-deoxy deamido bleomycin A2 + NH3
recombinant enzyme shows rapid and efficient hydrolysis of all bleomycins tested, exhibiting a superior catalytic efficiency for bleomycin B2
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6'-deoxy bleomycin Z + H2O
6'-deoxy deamido bleomycin Z + NH3
recombinant enzyme shows rapid and efficient hydrolysis of all bleomycins tested, exhibiting a superior catalytic efficiency for bleomycin B2
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amyloid peptide Abeta1-40 + H2O
peptide fragments
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processing by cleavage at bonds His14-Gln15 and Phe19-Phe20, endopeptidase activity, substrate preparation, overview
product determination by MALDI-TOF mass spectrometry
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?
amyloid peptide Abeta1-42 + H2O
peptide fragments
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processing by cleavage at bonds His14-Gln15 and Phe19-Phe20, endopeptidase activity, substrate preparation, overview
product determination by MALDI-TOF mass spectrometry
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?
bleomycin Z + H2O
deamido bleomycin Z + NH3
recombinant enzyme shows rapid and efficient hydrolysis of all bleomycins tested, exhibiting a superior catalytic efficiency for bleomycin B2
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citrulline-4-methylcoumarin 7-amide + H2O
citrulline + 7-amino-4-methylcoumarin
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citrulline-7-amido-4-methylcoumarin + H2O
citrulline + 7-amino-4-methylcoumarin
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huntingtin + H2O
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the enzyme is involved in a specific cleavage step at the N-terminal fragment cp-2 site of huntingtin
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L-Arg-7-amido-4-methylcoumarin + H2O
L-Arg + 7-amino-4-methylcoumarin
protease activity of mutant variants determined using substrate concentrations ranging from 0 to 0.125 mM
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L-tyrosine-p-nitroanilide + H2O
L-tyrosine + 4-nitroaniline
72% of activity with phenylalanine-betanitroanilide
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phenylalanine-betanaphthylamide + H2O
beta-naphthylamin + phenylalanine
best substrate
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phenylalanine-p-nitroanilide + H2O
p-nitroaniline + phenylalanine
activity comparable to phenylalanine-betanitroanilide
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Z-Leu-Leu-Glu-NH-4-nitroanilide + H2O
Z-Leu-Leu-Glu + 4-nitroaniline
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no activity in vitro due to requirement of binding to DNA-recognition sites of ztranscriptional activator Gal4p
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bleomycin + H2O
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bleomycin is a cytotoxic agent inducing pneumonitis, detoxification reaction
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bleomycin + H2O
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detoxification reaction, high enzyme expression level leads to resistance against the drug
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deamido bleomycin A2 + NH3
the enzyme hydrolyzes bleomycins into the biologically inactive deamido bleomycins
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bleomycin A2 + H2O
deamido bleomycin A2 + NH3
recombinant enzyme shows rapid and efficient hydrolysis of all bleomycins tested, exhibiting a superior catalytic efficiency for bleomycin B2
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deamido bleomycin B2 + NH3
the enzyme hydrolyzes bleomycins into the biologically inactive deamido bleomycins
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bleomycin B2 + H2O
deamido bleomycin B2 + NH3
recombinant enzyme shows rapid and efficient hydrolysis of all bleomycins tested, exhibiting a superior catalytic efficiency for bleomycin B2
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citrulline-beta-naphthylamide + H2O
citrulline + beta-naphthylamine
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neutral cysteine protease bleomycin hydrolase is essential for the breakdown of deiminated filaggrin into amino acids
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deiminated filaggrin + H2O
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recombinant human filaggrin is a component of the cornified cell envelope and the precursor of free amino acids acting as a natural moisturizing factor in the stratum corneum. Profilaggrin is synthesized as a large, extremely insoluble phosphoprotein. Deimination is critical for the degradation of filaggrin into free amino acids, deimination of filaggrin is catalyzed by murine PAD3
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deiminated filaggrin + H2O
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neutral cysteine protease bleomycin hydrolase is essential for the breakdown of deiminated filaggrin into amino acids
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deiminated filaggrin + H2O
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recombinant human filaggrin is a component of the cornified cell envelope and the precursor of free amino acids acting as a natural moisturizing factor in the stratum corneum. Profilaggrin is synthesized as a large, extremely insoluble phosphoprotein. Deimination is critical for the degradation of filaggrin into free amino acids, deimination of filaggrin is catalyzed by murine PAD3
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additional information
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the enzyme exhibits protection against homocysteine toxicity, role and mechanisms of bleomycin hydrolase, overview
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additional information
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the substrate specificity is controlled by the opening of the barrel structure and the positioning of the enzyme's C-terminus in the active site as opposed to the features of the substrate, mechanism, overview
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additional information
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bleomycin hydrolase as an essential component of chemotherapy regimens for disseminated testicular germ-cell cancer analyzed, study on relation of single nucleotide polymorphism (SNP) A1450G of the bleomycin hydrolase gene with survival according to genotype analyzed
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additional information
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bleomycin hydrolase as an essential component of chemotherapy regimens for disseminated testicular germ-cell cancer analyzed, study on relation of single nucleotide polymorphism (SNP) A1450G of the bleomycin hydrolase gene with survival according to genotype analyzed
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additional information
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bleomycin hydrolase is a neutral cysteine protease, the enzyme releases various amino acids except Pro from beta-naphthylamide derivatives and hydrolyzed citrulline-beta-naphthylamide most effectively, overview
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additional information
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role in generating MHC class I-presented peptides suggested
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additional information
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immunohistochemical analysis and behavioral phenotyping of mice with a targeted deletion of the neutral cysteine protease described
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additional information
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role of bleomycin hydrolase in antigen presentation and in generation of CD8 T cell response analyzed in bleomycin hydrolase-deficient mice
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additional information
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bleomycin hydrolase does not hydrolyze D-Hcy-thiolactone
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additional information
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the substrate specificity is controlled by the opening of the barrel structure and the positioning of the enzyme's C-terminus in the active site as opposed to the features of the substrate, mechanism, overview
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additional information
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the enzyme is a neutral cysteine protease, processing specificity on amyloid bet-peptides depends on the substrate structure and sequence, overview
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additional information
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the substrate specificity is controlled by the opening of the barrel structure and the positioning of the enzyme's C-terminus in the active site as opposed to the features of the substrate, mechanism, overview
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additional information
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bleomycin hydrolase is a neutral cysteine protease, the enzyme releases various amino acids except Pro from beta-naphthylamide derivatives and hydrolyzed citrulline-beta-naphthylamide most effectively, overview
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additional information
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the enzyme exhibits protection against homocysteine toxicity, role and mechanisms of bleomycin hydrolase, overview
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additional information
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the enzyme expression is regulated by galactose and Gal4p,expression pattrern
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