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
-
luteinizing
- paraoxonase
- thiolactone
- helveticus
- peplomycin
-
lutropins
- corneocytes
-
homocysteinylation
- beta-naphthylamide
- medicine
-
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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Engineering
Engineering on EC 3.4.22.40 - bleomycin hydrolase
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C73S
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ectopic expression of enzyme increases the secretion of amyloid precursor protein, increase is blocked in mutant
truncated C-terminus
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C-terminus is essential for protection against bleomycin induced chromatin breaks
V443I
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the naturally occurring polymorphism of the gene encoding the enzyme is associated to sporadic Alzheimer's disease and to the amyloid precursor protein
H369A
N392A
structural and catalytic effects of mutations summarized
additional information
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naturally occurring polymorphism A1450G in the BMH gene, causing a C-terminal amino acid substitution, is not responsible for development of bleomycin-induced pneumonitis, overview
additional information
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mutant pre3-2 is inactive with substrate Z-Leu-Leu-Glu-NH-4-nitroanilide, but can be complemented b ythe wild-type gene