Crystal structure of human bleomycin hydrolase, a self-compartmentalizing cysteine protease (Q27619037)

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F Gonzalez

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W Zheng

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S A Johnston

The neutral cysteine protease bleomycin hydrolase is essential for epidermal integrity and bleomycin resistance

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language of work or name

English

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publication date

15 June 1999

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published in

Structure

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volume

7

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issue

6

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page(s)

619-27

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cites work

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Bleomycin hydrolase is associated with risk of sporadic Alzheimer's disease

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Characterization and expression of the Lactobacillus helveticus pepC gene encoding a general aminopeptidase

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Characterization of the Lactobacillus helveticus CNRZ32 pepC gene

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Gene cloning and characterization of PepC, a cysteine aminopeptidase from Streptococcus thermophilus, with sequence similarity to the eucaryotic bleomycin hydrolase.

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Complete Genome Sequence of Treponema pallidum, the Syphilis Spirochete

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A yeast gene (BLH1) encodes a polypeptide with high homology to vertebrate bleomycin hydrolase, a family member of thiol proteinases.

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Separation of the protective enzyme bleomycin hydrolase from rabbit pulmonary aminopeptidases

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cDNA cloning and expression of chicken aminopeptidase H, possessing endopeptidase as well as aminopeptidase activity

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Human bleomycin hydrolase: molecular cloning, sequencing, functional expression, and enzymatic characterization

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Cloning and analysis of cDNA encoding rat bleomycin hydrolase, a DNA-binding cysteine protease

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Crystal structure of a conserved protease that binds DNA: the bleomycin hydrolase, Gal6

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Self-compartmentalizing proteases.

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The proteasome: paradigm of a self-compartmentalizing protease

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The unusual active site of Gal6/bleomycin hydrolase can act as a carboxypeptidase, aminopeptidase, and peptide ligase

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The cysteine-peptidase bleomycin hydrolase is a member of the galactose regulon in yeast

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Essential binding and functional domains of human bleomycin hydrolase

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Mapping the active site of papain with the aid of peptide substrates and inhibitors

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The nucleic acid binding activity of bleomycin hydrolase is involved in bleomycin detoxification

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Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 A resolution

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