Activation of chitin synthetase from Phycomyces blakesleeanus by calcium and calmodulin |
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Authors: | G Martinez-Cadena J Ruiz-Herrera |
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Institution: | (1) Instituto de Investigacion en Biologia Experimental, Facultad de Quimica, Universidad de Guanajuato, Guanajuato, Mexico;(2) Departmento de Genetica y Biologia Molecular, Centro de Investigacion y Estudios Avanzados I.P.N., Mexico |
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Abstract: | Levels of basal chitin synthetase in cell-free extracts from Phycomyces blakesleeanus were reduced by breakage of cells in the presence of EDTA or EGTA. Addition of Ca2+ to these extracts activated chitin synthetase. Maximal activation was obtained after 2 h at a Ca2+ concentration of 2–5 mM. Activation by calcium was not reduced by any protease inhibitor tested but benzamidine, whereas the weak proteolytic activity of the extracts was inhibited by antipain. Larger levels of chitin synthetase activation were obtained by the simultaneous addition of calcium and calmodulin in most, but not all extracts. This further activation by calmodulin was prevented by TFP. ATP or cAMP did not stimulate activation by calcium or calcium-calmodulin.Abbreviations EGTA
ethylene glycol-bis(B-aminoethylether)-N,N N -tetraacetic acid
- GlcNAc
N-acetyl-d-glucosamine
- PMSF
phenylmethylsulfonyl fluoride
- SBTI
soybean trypsin inhibitor
- TFP
trifluoperazine
- TLCK
N-p-tosyl-l-lysine choromethyl ketone
- UDPGlcNAc
uridine diphosphate N-acetyl-d-glucosamine |
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Keywords: | Chitin synthetase Phycomyces blakesleeanus Calcium-calmodulin Proteases |
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