TY - JOUR
T1 - Identification of novel β-mannan- and β-glucan-binding modules
T2 - Evidence for a superfamily of carbohydrate-binding modules
AU - Sunna, A.
AU - Gibbs, M. D.
AU - Bergquist, P. L.
PY - 2001/6/15
Y1 - 2001/6/15
N2 - Many glycoside hydrolases, which degrade long-chain carbohydrate polymers, possess distinct catalytic modules and non-catalytic carbohydrate-binding modules (CBMs). On the basis of conserved protein secondary structure, we describe here the identification and experimental characterization of novel type of mannanase-associated mannan-binding module and also characterization of two CBM family 4 laminarinase-associated β-glucan-binding modules. These modules are predicted to belong to a superfamily of CBMs which include families 4, 16, 17, 22 and a proposed new family, family 27.
AB - Many glycoside hydrolases, which degrade long-chain carbohydrate polymers, possess distinct catalytic modules and non-catalytic carbohydrate-binding modules (CBMs). On the basis of conserved protein secondary structure, we describe here the identification and experimental characterization of novel type of mannanase-associated mannan-binding module and also characterization of two CBM family 4 laminarinase-associated β-glucan-binding modules. These modules are predicted to belong to a superfamily of CBMs which include families 4, 16, 17, 22 and a proposed new family, family 27.
UR - http://www.scopus.com/inward/record.url?scp=0035875574&partnerID=8YFLogxK
U2 - 10.1042/0264-6021:3560791
DO - 10.1042/0264-6021:3560791
M3 - Article
C2 - 11389686
AN - SCOPUS:0035875574
VL - 356
SP - 791
EP - 798
JO - The Biochemical journal
JF - The Biochemical journal
SN - 0264-6021
IS - 3
ER -