Abstract:
:The enzymatic degradation of the closely related insoluble polysaccharides; cellulose (β(1-4)-linked glucose) by cellulases and chitin (β(1-4)-linked N-acetylglucosamine) by chitinases, is of large biological and economical importance. Processive enzymes with different inherent directionalities, i.e. attacking the polysaccharide chains from opposite ends, are crucial for the efficiency of this degradation process. While processive cellulases with complementary functions differ in structure and catalytic mechanism, processive chitinases belong to one single protein family with similar active site architectures. Using the unique model system of Serratia marcescens with two processive chitinases attacking opposite ends of the substrate, we here show that different directionalities of processivity are correlated to distinct differences in the kinetic signatures for hydrolysis of oligomeric tetra-N-acetyl chitotetraose.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Hamre AG,Schaupp D,Eijsink VG,Sørlie Mdoi
10.1016/j.febslet.2015.05.034subject
Has Abstractpub_date
2015-07-08 00:00:00pages
1807-12issue
15eissn
0014-5793issn
1873-3468pii
S0014-5793(15)00428-7journal_volume
589pub_type
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