Structural consequences of neopullulanase mutations

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Structural consequences of neopullulanase mutations. / Lamminmaki, U; Vihinen, Mauno.

In: BBA - Protein Structure and Molecular Enzymology, Vol. 1295, No. 2, 1996, p. 195-200.

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TY - JOUR

T1 - Structural consequences of neopullulanase mutations

AU - Lamminmaki, U

AU - Vihinen, Mauno

PY - 1996

Y1 - 1996

N2 - Bacillus stearothermophilus neopullulanase (NPL) structure was modeled based on Aspergillus oryzae alpha-amylase (TAA) to understand the structure-function relationships of this pullulan hydrolyzing enzyme. The NPL structure seems to consist of a central (alpha/beta)(8) barrel to which the other domains are attached. The immediate surroundings of the NPL catalytic site were found to have very similar structure to TAA. The more distant sites are different due to the stereochemical requirements of accommodating in the substrate alpha-1,6-linkages at every third position instead of alpha-1,4-linkages. The substrate binding cleft is wider than in alpha-amylases. The NPL structure, function, substrate binding and the consequences of mutations were discussed based on the modeled structure.

AB - Bacillus stearothermophilus neopullulanase (NPL) structure was modeled based on Aspergillus oryzae alpha-amylase (TAA) to understand the structure-function relationships of this pullulan hydrolyzing enzyme. The NPL structure seems to consist of a central (alpha/beta)(8) barrel to which the other domains are attached. The immediate surroundings of the NPL catalytic site were found to have very similar structure to TAA. The more distant sites are different due to the stereochemical requirements of accommodating in the substrate alpha-1,6-linkages at every third position instead of alpha-1,4-linkages. The substrate binding cleft is wider than in alpha-amylases. The NPL structure, function, substrate binding and the consequences of mutations were discussed based on the modeled structure.

KW - neopullulanase

KW - structure-function relationship

KW - molecular modeling

KW - substrate binding

KW - active site

KW - (B-stearothermophilus)

KW - (A-oryzae)

U2 - 10.1016/0167-4838(96)00040-4

DO - 10.1016/0167-4838(96)00040-4

M3 - Article

VL - 1295

SP - 195

EP - 200

JO - Biochimica et Biophysica Acta - Proteins and Proteomics

JF - Biochimica et Biophysica Acta - Proteins and Proteomics

SN - 1570-9639

IS - 2

ER -