The disulphide bridges in a cellobiohydrolase and an endoglucanase from Trichoderma reesei

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Abstract
The positions of the disulfide bridges of the 1,4-.beta.-glucan cellobiohydrolase (CBH I) of the fungus T. reesei were investigated. The enzyme contains 12 disulfide bridges and no free cysteine residues. The location of 6 disulfide bridges were determiend experimentally. The bonding patterns of the 2 disulfide bridges in the C-terminal region is suggested on the basis of internal homology. The remaining 4 disulfide bridges are put into 2 groups, each containing 4 half-cystine residues where 2 are adjacent. A repeating bonding pattern is observed along the peptide chain and a non-local disulfide bond with an unusually long separation distance links the N-terminal and the C-terminal region. The disulfide-bonded CNBr [cyanogen bromide] peptides of a 1,4-.beta.-glucan glucanohydrolase (endoglucanase II) from T. reesei were isolated and a disulfide bonding pattern is suggested on the basis of the sequence homology between the 2 enzymes.

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