Title of article :
Carbohydrate esterase family 4 enzymes: substrate specificity
Author/Authors :
Frederic Caufrier، نويسنده , , Aggeliki Martinou، نويسنده , , Claude Dupont، نويسنده , , Vassilis Bouriotis، نويسنده ,
Issue Information :
دوهفته نامه با شماره پیاپی سال 2003
Pages :
6
From page :
687
To page :
692
Abstract :
The substrate specificity of selected enzymes classified under Carbohydrate Esterase family 4 (CE4) has been examined. Chitin deacetylase from Mucor rouxii and both a native and a truncated form of acetyl xylan esterase from Streptomyces lividans were found to be active on both xylan and several soluble chitinous substrates. Furthermore, the activities of all enzymes examined were significantly increased in the presence of Co2+ when chitinous substrates were employed. However, the presence of this metal ion did not result in enhancing the activities of the enzymes when xylan was used as substrate. An acetyl xylan esterase from Bacillus pumilus, classified under Carbohydrate Esterase family 7, was found to be inactive towards all chitinous substrates tested. Finally, all enzymes examined were inactive towards cell wall peptidoglycan.
Keywords :
Chitin , Acetyl xylan esterase , Peptidoglycan , Xylan , Chitin deacetylase
Journal title :
Carbohydrate Research
Serial Year :
2003
Journal title :
Carbohydrate Research
Record number :
963693
Link To Document :
بازگشت