Abstract
Cellobiohydrolase I (CBH I), the major component of Trichoderma reesei cellulolytic system, is comprised of a catalytic core domain joined to a cellulose binding-domain (CBD) by an extended O-glycosylated interdomain linker peptide. Two internal deletions were introduced to the linker in order to investigate its function particularly in the hydrolysis of crystalline cellulose. Deletion of the first one-third of the linker, including a putative hinge region, reduces the binding capacity of CBH I in high enzyme coverage but does not affect its enzymatic activity on crystalline cellulose. The longer deletion removing practically all of the linker dramatically reduces the rate of crystalline cellulose degradation even though the enzyme still binds to the substrate. We conclude that sufficient spatial separation of the two domains is required for efficient function of CBH I. It is evident that the presence of a functional CBD is increasingly important for CBH I toward higher enzyme to cellulose ratios. Our data suggest that the putative hinge removed by the first deletion facilitates CBD-driven binding and dense packing of the wild type enzyme on the cellulose surface.
| Original language | English |
|---|---|
| Pages (from-to) | 20756-20761 |
| Number of pages | 6 |
| Journal | Journal of Biological Chemistry |
| Volume | 268 |
| Issue number | 28 |
| Publication status | Published - 1 Jan 1993 |
| MoE publication type | A1 Journal article-refereed |
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Role of the interdomain linker peptide of Trichoderma reesei cellobiohydrolase I in its interaction with crystalline cellulose. / Srisodsuk, Malee; Reinikainen, T.; Penttila, M.; Teeri, Tuula T.
In: Journal of Biological Chemistry, Vol. 268, No. 28, 01.01.1993, p. 20756-20761.Research output: Contribution to journal › Article › Scientific › peer-review
TY - JOUR
T1 - Role of the interdomain linker peptide of Trichoderma reesei cellobiohydrolase I in its interaction with crystalline cellulose
AU - Srisodsuk, Malee
AU - Reinikainen, T.
AU - Penttila, M.
AU - Teeri, Tuula T.
PY - 1993/1/1
Y1 - 1993/1/1
N2 - Cellobiohydrolase I (CBH I), the major component of Trichoderma reesei cellulolytic system, is comprised of a catalytic core domain joined to a cellulose binding-domain (CBD) by an extended O-glycosylated interdomain linker peptide. Two internal deletions were introduced to the linker in order to investigate its function particularly in the hydrolysis of crystalline cellulose. Deletion of the first one-third of the linker, including a putative hinge region, reduces the binding capacity of CBH I in high enzyme coverage but does not affect its enzymatic activity on crystalline cellulose. The longer deletion removing practically all of the linker dramatically reduces the rate of crystalline cellulose degradation even though the enzyme still binds to the substrate. We conclude that sufficient spatial separation of the two domains is required for efficient function of CBH I. It is evident that the presence of a functional CBD is increasingly important for CBH I toward higher enzyme to cellulose ratios. Our data suggest that the putative hinge removed by the first deletion facilitates CBD-driven binding and dense packing of the wild type enzyme on the cellulose surface.
AB - Cellobiohydrolase I (CBH I), the major component of Trichoderma reesei cellulolytic system, is comprised of a catalytic core domain joined to a cellulose binding-domain (CBD) by an extended O-glycosylated interdomain linker peptide. Two internal deletions were introduced to the linker in order to investigate its function particularly in the hydrolysis of crystalline cellulose. Deletion of the first one-third of the linker, including a putative hinge region, reduces the binding capacity of CBH I in high enzyme coverage but does not affect its enzymatic activity on crystalline cellulose. The longer deletion removing practically all of the linker dramatically reduces the rate of crystalline cellulose degradation even though the enzyme still binds to the substrate. We conclude that sufficient spatial separation of the two domains is required for efficient function of CBH I. It is evident that the presence of a functional CBD is increasingly important for CBH I toward higher enzyme to cellulose ratios. Our data suggest that the putative hinge removed by the first deletion facilitates CBD-driven binding and dense packing of the wild type enzyme on the cellulose surface.
UR - http://www.scopus.com/inward/record.url?scp=0027372765&partnerID=8YFLogxK
M3 - Article
C2 - 8407900
AN - SCOPUS:0027372765
VL - 268
SP - 20756
EP - 20761
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
SN - 0021-9258
IS - 28
ER -