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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/3853073
- author
- Lamminmaki, U
and Vihinen, Mauno
LU
- publishing date
- 1996
- 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
- 2016-04-01 15:57:46
- date last changed
- 2022-01-28 08:22:22
@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}},
keywords = {{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}},
doi = {{10.1016/0167-4838(96)00040-4}},
volume = {{1295}},
year = {{1996}},
}