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

Lysyl oxidase copper-talon complex: a model

C J Krebs1, S A Krawetz

  • 1Department of Molecular Biology and Genetics, Wayne State University School of Medicine, Detroit, MI 48201.

Biochimica Et Biophysica Acta
|September 3, 1993
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

Phthalates impact on the epigenetic factors contributed specifically by the father at fertilization.

Epigenetics & chromatin·2023
Same author

Improving the assessment of predator functional responses by considering alternate prey and predator interactions.

Ecology·2017
Same author

Effects of extra food on Peromyscus and Clethrionomys populations in the southern Yukon.

Oecologia·2017
Same author

Can predation cause the 10-year hare cycle?

Oecologia·2017
Same author

Mammalian cycles: internally defined periods and interaction-driven amplitudes.

PeerJ·2015
Same author

Are big mammals simply little mammals writ large?

Oecologia·2014
Same journal

Cumulative Contents.

Biochimica et biophysica acta·2020
Same journal

Molecular Basis of Disease Cumulative Contents.

Biochimica et biophysica acta·2020
Same journal

General Subjects Cumulative Contents.

Biochimica et biophysica acta·2020
Same journal

Erratum to 'on the role of exchangeable hydrogen bonds for the kinetics of P680<sup>+·</sup> Q<sub>A</sub> <sup>-·</sup> formation and P680<sup>+·</sup> Pheo<sup>-·</sup> recombination in photosystem II' [Biochim. Biophys. Acta 1276 (1996) 35-44].

Biochimica et biophysica acta·2019
Same journal

Oligomeric state of the light-harvesting complexes B800-850 and B875 from purple bacterium Rubrivivax gelatinosus in detergent solution.

Biochimica et biophysica acta·2019
Same journal

Regulation of pigment content and enzyme activity in the cyanobacterium Nostoc sp. Mac grown in continuous light, a light-dark photoperiod, or darkness.

Biochimica et biophysica acta·2019
See all related articles

Computer analysis revealed highly conserved structures in lysyl oxidase enzymes across species. A structural model highlights a copper talon active site, aiding in understanding enzyme function.

Area of Science:

  • Biochemistry and Molecular Biology
  • Structural Biology
  • Enzymology

Background:

  • Lysyl oxidase (LOX) is a crucial enzyme involved in extracellular matrix cross-linking.
  • Understanding LOX structure is vital for deciphering its role in physiological and pathological processes.

Purpose of the Study:

  • To compare primary and secondary structures of lysyl oxidase across species.
  • To develop a structural model for the mature lysyl oxidase enzyme.
  • To identify key structural features, including the active site.

Main Methods:

  • Comparative analysis of translated amino acid sequences from human, rat, and mouse lysyl oxidase cDNAs.
  • Computer-based prediction of protein secondary structures.
  • Reconciliation of a prototypical structural model with known enzyme properties.

Related Experiment Videos

Main Results:

  • Highly conserved primary and predicted secondary structures were identified across human, rat, and mouse lysyl oxidase.
  • A structural model of mature lysyl oxidase was developed.
  • A copper coordination complex, resembling a talon, was proposed as part of the active site.

Conclusions:

  • The conserved structure suggests a fundamental role for lysyl oxidase across mammalian species.
  • The proposed structural model, including the copper talon active site, provides a framework for future research.
  • This model facilitates the elucidation of structure-function relationships within the lysyl oxidase enzyme.