ArticleThe Journal of biological chemistry2011
Crystal structures of protein glutaminase and its pro forms converted into enzyme-substrate complex.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 13 papers.
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13 citing papers in PubMed.
- Enzymatic Deamidation of Plant Proteins by Protein-Glutamine Glutaminases: Effects on Solubility, Foaming and Emulsion Properties.Foods (Basel, Switzerland) · 2026Article
- Toward food-grade production of the Bacteroides helcogenes protein-glutamine glutaminase with an optimized Bacillus subtilis strain.Applied microbiology and biotechnology · 2026Article
- Identification of novel toxins associated with the extracellular contractile injection system using machine learning.Molecular systems biology · 2024Article
- Purified protein glutaminase fromFood chemistry: X · 2024Article
- Identification and classification of papain-like cysteine proteinases.The Journal of biological chemistry · 2023Article
- L-Glutamine-, peptidyl- and protein-glutaminases: structural features and applications in the food industry.World journal of microbiology & biotechnology · 2022Review
- The characteristics of protein-glutaminase from an isolatedFrontiers in microbiology · 2022Article
- Lasso Proteins-Unifying Cysteine Knots and Miniproteins.Polymers · 2021Article
- Eight Kinetically Stable but Thermodynamically Activated Molecules that Power Cell Metabolism.Chemical reviews · 2018Review
- Serial deletion reveals structural basis and stability for the core enzyme activity of human glutaminase 1 isoforms: relevance to excitotoxic neurodegeneration.Translational neurodegeneration · 2017Article
- Crystal structure of human protein N-terminal glutamine amidohydrolase, an initial component of the N-end rule pathway.PloS one · 2014Article
- Structural mechanism of ubiquitin and NEDD8 deamidation catalyzed by bacterial effectors that induce macrophage-specific apoptosis.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Structure of the catalytic domain of the Salmonella virulence factor SseI.Acta crystallographica. Section D, Biological crystallography · 2012Article
Corrections and comments
- Erratum issued
Authors and funding
9 authors.
Funding
No grant is acknowledged in the PubMed record.
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.
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