The Calvin cycle in cyanobacteria is regulated by CP12 via the NAD(H)/NADP(H) ratio under light/dark conditions.
- M. Tamoi, T. Miyazaki, T. Fukamizo, S. Shigeoka
- BiologyThe Plant Journal
- 1 April 2005
Under light and dark conditions, the oligomerization of CP12 with PRK and GAPDH regulates the activities of both enzymes and thus the carbon flow from the Calvin cycle to the oxidative pentose phosphate cycle.
The Arabidopsis CERK1‐associated kinase PBL27 connects chitin perception to MAPK activation
- Kenta Yamada, K. Yamaguchi, T. Kawasaki
- BiologyEMBO Journal
- 27 September 2016
A complete phospho‐signaling transduction pathway from PRR‐mediated pathogen recognition to MAPK activation in plants is identified and genetic evidence suggests that phosphorylation of MAPKKK5 by PBL27 is essential for chitin‐induced MAPKactivation in plants.
Chitinolytic enzymes: catalysis, substrate binding, and their application.
- T. Fukamizo
- Chemistry, BiologyCurrent protein and peptide science
- 30 June 2000
The functional diversity of the chitinolytic enzymes might be related to different physiological functions of the enzymes, and recent understanding of the catalytic and substrate binding mechanisms would be helpful for arrangement of a powerful strategy in such an application.
Novel Chitosanase from Streptomyces griseus HUT 6037 with Transglycosylation Activity
- T. Tanabe, Kazuko Morinaga, T. Fukamizo, M. Mitsutomi
- BiologyBioscience, biotechnology and biochemistry
- 1 January 2003
This is the first report of a family 5 chitosanase with transglycosylation activity, and these enzymes catalyzed a glycosyltransfer reaction in the hydrolysis of chitooligosaccharides.
Chitinase Gene Expression in Response to Environmental Stresses in Arabidopsis thaliana: Chitinase Inhibitor Allosamidin Enhances Stress Tolerance
- Y. Takenaka, S. Nakano, M. Tamoi, S. Sakuda, T. Fukamizo
- Environmental Science, BiologyBioscience, biotechnology and biochemistry
- 23 May 2009
Interestingly, the plants treated with allosamidin were more tolerant of abiotic stresses (cold, freezing, heat, and strong light) than the control plants, and it appeared that allosamsidin enhances AtChiA and AtchiB expression under heat and strongLight stresses.
A class V chitinase from Arabidopsis thaliana: gene responses, enzymatic properties, and crystallographic analysis
- T. Ohnuma, T. Numata, T. Fukamizo
- BiologyPlanta
- 9 March 2011
All of the structural and functional properties of AtChiC are quite similar to those obtained for NtChiV, and seem to be common to class V chitinases from higher plants.
Chitosanase from Streptomyces sp. strain N174: a comparative review of its structure and function.
- T. Fukamizo, R. Brzezinski
- Biology, ChemistryBiochemistry and cell biology = Biochimie et…
- 1997
Structural and functional similarities were found between chitosanase, barley chitinase, bacteriophage T4 lyso enzyme, and goose egg white lysozyme, even though these proteins share no sequence similarities.
Disruption of the gene encoding the ChiB1 chitinase of Aspergillus fumigatus and characterization of a recombinant gene product.
- A. Jaques, T. Fukamizo, D. Adams
- BiologyMicrobiology
- 1 October 2003
The gene encoding a major, inducible 45 kDa chitinase of Aspergillus fumigatus was cloned and analysis of the deduced amino acid sequence identified a chit inase of the fungal/bacterial class which was designated ChiB1, which was shown to function by a retaining mechanism of action.
Two exo-beta-D-glucosaminidases/exochitosanases from actinomycetes define a new subfamily within family 2 of glycoside hydrolases.
- Nathalie Côté, A. Fleury, Émilie Dumont-Blanchette, T. Fukamizo, M. Mitsutomi, R. Brzezinski
- Biology, ChemistryBiochemical Journal
- 15 March 2006
The SAV1223 protein from Streptomyces avermitilis has been purified following gene cloning and expression in a heterologous host and shown to be a GlcNase with no detectable beta-mannosidase activity.
Reaction mechanism of chitosanase from Streptomyces sp. N174.
- T. Fukamizo, Y. Honda, S. Goto, I. Boucher, R. Brzezinski
- Biology, ChemistryBiochemical Journal
- 15 October 1995
It is most likely that the substrate-binding cleft of the chitosanase can accommodate at least six GlcN residues, and that the cleavage point is located at the midpoint of the binding cleft.
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