The Unusual Active Site of Gal6/Bleomycin Hydrolase Can Act as a Carboxypeptidase, Aminopeptidase, and Peptide Ligase

The Unusual Active Site of Gal6/Bleomycin Hydrolase Can Act as a Carboxypeptidase, Aminopeptidase, and Peptide Ligase

Source :

• Cell [ 0092-8674 ] ; 1998.

English descriptors

• Teeft :
  • Acta cryst, Active site, Active site cleft, Active site cleft region, Active site clefts, Active site cysteine, Active sites, Amide bond, Amino, Amino acid increments, Amino acids, Amino terminus, Aminopeptidase, Aminopeptidase activity, Bacterial bleomycin hydrolase, Biol, Bleomycin, Bleomycin hydrolase, Bleomycin hydrolysis, Bond angles, Bond lengths, Carboxylate, Carboxylate oxygens, Carboxypeptidase, Carboxypeptidase activity, Catalytic residues, Cell dimensions, Central channel, Cleavage, Cleavage site, Crystal structure, Cysteine, Cysteine protease, Cysteine proteinase, Data collection, Deletion, Deletion variants, Dihedral angles, Drop vapor diffusion method, Electron density, Electron density maps, Electrospray mass spectrometry, Endopeptidase, Endopeptidase activity, Equal amounts, Gal6, Gal6p, Gene fragment, Human bleomycin hydrolase, Hydrolase, Ionic interactions, Last shell, Leupeptin, Lysine, Mass spectrometry, Molecular mass, Molecular ruler, Mutant, Mutant protein, Mutant proteins, National institutes, National synchrotron light source, Nucleic acid binding activity, Nucleophilic cysteine, Other proteases, Oxyanion hole, Peptidase, Peptidase activity, Peptide, Peptide substrate, Positional specificity, Protease, Proteasome, Protein solution, Protein structures, Ramachandran plot, Research imaging plate detector system, Reservoir solution, Side chain, Single crystal, Substrate specificity, Terminus, Terminus controls, Tris buffer, Variant, Wild type, Zheng.

Abstract

• https://api.istex.fr/ark:/67375/6H6-7RX1W659-8/fulltext.pdf

Affiliations:

• États-Unis

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