Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Structural consequences of neopullulanase mutations

U Lamminmäki1, M Vihinen

  • 1Center for Structural Biochemistry, Karolinska Institute, NOVUM, Huddinge, Sweden.

Biochimica Et Biophysica Acta
|July 18, 1996
PubMed
Summary
This summary is machine-generated.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Substitution scanning identifies a novel, catalytically active ibrutinib-resistant BTK cysteine 481 to threonine (C481T) variant.

Leukemia·2016
Same author

Synthetic single-framework antibody library integrated with rapid affinity maturation by VL shuffling.

Protein engineering, design & selection : PEDS·2011
Same author

Somatic mutation databases as tools for molecular epidemiology and molecular pathology of cancer: proposed guidelines for improving data collection, distribution, and integration.

Human mutation·2008
Same author

Recommendations for locus-specific databases and their curation.

Human mutation·2007
Same author

A structured simple form for ordering genetic tests is needed to ensure coupling of clinical detail (phenotype) with DNA variants (genotype) to ensure utility in publication and databases.

Human mutation·2007
Same author

The structural basis of hyper IgM deficiency - CD40L mutations.

Protein engineering, design & selection : PEDS·2007

Bacillus stearothermophilus neopullulanase (NPL) structure was modeled using alpha-amylase as a template. This reveals differences in substrate binding crucial for hydrolyzing pullulan, impacting enzyme function and mutation effects.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Enzymology

Background:

  • Pullulanase enzymes are crucial for carbohydrate metabolism.
  • Understanding neopullulanase (NPL) structure-function relationships is key to enzyme engineering.

Purpose of the Study:

  • To model the three-dimensional structure of Bacillus stearothermophilus neopullulanase (NPL).
  • To elucidate the structure-function relationships of NPL, a pullulan-hydrolyzing enzyme.
  • To compare NPL structure with Aspergillus oryzae alpha-amylase (TAA).

Main Methods:

  • Homology modeling of NPL based on the TAA structure.
  • Analysis of catalytic site and substrate-binding cleft similarities and differences.

Main Results:

Related Experiment Videos

  • The modeled NPL structure features a central (alpha/beta)8 barrel with attached domains.
  • The catalytic site environment of NPL closely resembles that of TAA.
  • Divergences in more distant regions accommodate NPL's specific substrate (alpha-1,6-linkages) compared to TAA (alpha-1,4-linkages).
  • The substrate-binding cleft in NPL is wider than in alpha-amylases.

Conclusions:

  • The modeled NPL structure provides insights into its unique substrate specificity.
  • Structural differences explain NPL's ability to hydrolyze alpha-1,6-linkages in pullulan.
  • The study facilitates understanding of NPL function and the impact of mutations.