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Structural consequences of neopullulanase mutations

Lamminmaki, U and Vihinen, Mauno LU (1996) In BBA - Protein Structure and Molecular Enzymology 1295(2). p.195-200
Abstract
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... (More)
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. (Less)
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author
publishing date
type
Contribution to journal
publication status
published
subject
keywords
neopullulanase, structure-function relationship, molecular modeling, substrate binding, active site, (B-stearothermophilus), (A-oryzae)
in
BBA - Protein Structure and Molecular Enzymology
volume
1295
issue
2
pages
195 - 200
publisher
Elsevier
external identifiers
  • wos:A1996UY02400010
  • scopus:0030592188
ISSN
0167-4838
DOI
10.1016/0167-4838(96)00040-4
language
English
LU publication?
no
id
ff2d901e-ef8f-465f-b0c1-a078523aecc8 (old id 3853073)
date added to LUP
2013-06-28 14:35:20
date last changed
2017-01-01 06:51:46
@article{ff2d901e-ef8f-465f-b0c1-a078523aecc8,
  abstract     = {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.},
  author       = {Lamminmaki, U and Vihinen, Mauno},
  issn         = {0167-4838},
  keyword      = {neopullulanase,structure-function relationship,molecular modeling,substrate binding,active site,(B-stearothermophilus),(A-oryzae)},
  language     = {eng},
  number       = {2},
  pages        = {195--200},
  publisher    = {Elsevier},
  series       = {BBA - Protein Structure and Molecular Enzymology},
  title        = {Structural consequences of neopullulanase mutations},
  url          = {http://dx.doi.org/10.1016/0167-4838(96)00040-4},
  volume       = {1295},
  year         = {1996},
}