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Information on EC 3.4.22.40 - bleomycin hydrolase and Organism(s) Saccharomyces cerevisiae and UniProt Accession Q01532

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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.22 Cysteine endopeptidases
                3.4.22.40 bleomycin hydrolase
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This record set is specific for:
Saccharomyces cerevisiae
UNIPROT: Q01532 not found.
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The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
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
blh, bleomycin hydrolase, blm hydrolase, htlase, homocysteine thiolactonase, aminopeptidase c, hcy-thiolactonase, aminopeptidase h, hydrolase h, bana-hydrolase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
aminopeptidase C
-
-
-
-
aminopeptidase H
-
-
-
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BANA-hydrolase
-
-
-
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Bleomycin hydrolase
-
-
-
-
Blh1p
-
-
-
-
BLM hydrolase
-
-
-
-
BMH
-
-
-
-
Gal6p
Hcy-thiolactonase
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the bleomycin hydrolase is identical with the homocysteine thiolactonase, overview
homocysteine thiolactonase
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the bleomycin hydrolase is identical with the homocysteine thiolactonase, overview
HTLase
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the bleomycin hydrolase is identical with the homocysteine thiolactonase, overview
hydrolase H
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-
-
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PEPC
-
-
-
-
yeast cysteine protease
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-
additional information
-
the enzyme belongs to the C1B peptidase family
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
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
show the reaction diagram
acts as carboxypeptidase, aminopeptidase and peptide ligase
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
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-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
53096-17-6
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
bleomycin + H2O
deamido-bleomycin
show the reaction diagram
-
-
-
?
L-Arg-7-amido-4-methylcoumarin + H2O
L-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
protease activity of mutant variants determined using substrate concentrations ranging from 0 to 0.125 mM
-
-
?
bleomycin + H2O
deamido-bleomycin
show the reaction diagram
Z-Leu-Leu-Glu-NH-4-nitroanilide + H2O
Z-Leu-Leu-Glu + 4-nitroaniline
show the reaction diagram
-
no activity in vitro due to requirement of binding to DNA-recognition sites of ztranscriptional activator Gal4p
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
Z-Leu-Leu-Glu-NH-4-nitroanilide + H2O
Z-Leu-Leu-Glu + 4-nitroaniline
show the reaction diagram
-
no activity in vitro due to requirement of binding to DNA-recognition sites of ztranscriptional activator Gal4p
-
-
?
additional information
?
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Arg-Ala
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86% inhibition of HLTase activity at 2 mM
Cd2+
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5% inhibition of HLTase activity 2 mM
Cu2+
-
9% inhibition of HLTase activity 2 mM
E64
-
99% inhibition of HLTase activity at 0.012 mM
H2O2
-
41% inhibition of HLTase activity 2 mM
iodoacetamide
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94% inhibition of HLTase activity 2 mM
Leu-Ala
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50% inhibition of HLTase activity at 2 mM
Lys-Ala
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77% inhibition of HLTase activity at 2 mM
Lys-Leu
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26% inhibition of HLTase activity at 2 mM
Zn2+
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70% inhibition of HLTase activity at 2 mM
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
galactose
transcripton regulator
Nucleic acids
-
RNA, single-stranded DNA or nicked DNA are bound
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
in the presence of Ca2+
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Manually annotated by BRENDA team
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging-drop method, structure and catalytic site of yeast bleomycin hydrolase indicated, structural changes at the active site of mutant variants shown, data collection, refinements and structural alignments between wild-type and mutant variants indicated
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H369A
structural and catalytic effects of mutations shown
H369L
structural and catalytic effects of mutations shown
N392A
structural and catalytic effects of mutations summarized
N392L
structural and catalytic effects of mutations shown
N392V
structural and catalytic effects of mutations shown
Q67E
structural and catalytic effects of mutations indicated
H369A
-
inactive mutant
additional information
-
mutant pre3-2 is inactive with substrate Z-Leu-Leu-Glu-NH-4-nitroanilide, but can be complemented b ythe wild-type gene
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
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recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography to homogeneity
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli, mutant generation described
expression in Escherichia coli
expression in Escherichia coli
-
expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
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gene YCP1 or BLH1, DNA sequence determination
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Niemer, I.; Mueller, G.; Strobel, G.; Bandlow, W.
Bleomycin hydrolase (Blh1p), a multi-sited thiol protease in search of a distinct physiological role
Curr. Genet.
32
41-51
1997
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Zheng, W.; Johnston, S.A.
The nucleic acid binding activity of bleomycin hydrolase is involved in bleomycin detoxification
Mol. Cell. Biol.
18
3580-3585
1998
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Zheng, W.; Xu, H.E.; Johnston, S.A.
The cysteine-peptidase bleomycin hydrolase is a member of the galactose regulon in yeast
J. Biol. Chem.
272
30350-30355
1997
Saccharomyces cerevisiae (Q01532), Saccharomyces cerevisiae
Manually annotated by BRENDA team
Zheng, W.; Johnston, S.A.; Joshua-Tor, L.
The unusual active site of Gal6/bleomycin hydrolase can act as a carboxypeptidase, aminopeptidase, and peptide ligase
Cell
93
103-109
1998
Saccharomyces cerevisiae (Q01532)
Manually annotated by BRENDA team
Joshua-Tor, L.; Johnston, S.A.
Bleomycin hydrolase
Handbook of Proteolytic Enzymes (Barrett, A. J. , Rawlings, N. D. , Woessner, J. F. , eds. )Academic Press
2
1197-1201
2004
Saccharomyces cerevisiae, Oryctolagus cuniculus, Homo sapiens, Rattus norvegicus, Streptomyces verticillus
-
Manually annotated by BRENDA team
Zimny, J.; Sikora, M.; Guranowski, A.; Jakubowski, H.
Protective mechanisms against homocysteine toxicity: the role of bleomycin hydrolase
J. Biol. Chem.
281
22485-22492
2006
Homo sapiens, Saccharomyces cerevisiae
Manually annotated by BRENDA team
OFarrell, P.A.; Joshua-Tor, L.
Mutagenesis and crystallographic studies of the catalytic residues of the papain family protease bleomycin hydrolase: new insights into active-site structure
Biochem. J.
401
421-428
2007
Saccharomyces cerevisiae (Q01532), Saccharomyces cerevisiae
Manually annotated by BRENDA team