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J Biol Chem ; 286(44): 38691-38702, 2011 Nov 04.
Article in English | MEDLINE | ID: mdl-21926168

ABSTRACT

Protein glutaminase, which converts a protein glutamine residue to a glutamate residue, is expected to be useful as a new food-processing enzyme. The crystal structures of the mature and pro forms of the enzyme were refined at 1.15 and 1.73 Å resolution, respectively. The overall structure of the mature enzyme has a weak homology to the core domain of human transglutaminase-2. The catalytic triad (Cys-His-Asp) common to transglutaminases and cysteine proteases is located in the bottom of the active site pocket. The structure of the recombinant pro form shows that a short loop between S2 and S3 in the proregion covers and interacts with the active site of the mature region, mimicking the protein substrate of the enzyme. Ala-47 is located just above the pocket of the active site. Two mutant structures (A47Q-1 and A47Q-2) refined at 1.5 Å resolution were found to correspond to the enzyme-substrate complex and an S-acyl intermediate. Based on these structures, the catalytic mechanism of protein glutaminase is proposed.


Subject(s)
Chryseobacterium/enzymology , Glutaminase/chemistry , Amino Acid Sequence , Catalysis , Catalytic Domain , Crystallization , Crystallography, X-Ray/methods , Cysteine Proteases/chemistry , Glutamine/chemistry , Molecular Sequence Data , Mutagenesis, Site-Directed , Mutation , Proline/chemistry , Protein Binding , Protein Conformation , Transglutaminases/chemistry
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