Cerqueira, NMFSA, Coelho C, Bras NF, Fernandes PA, Garattini E, Terao M, Romao MJ, Ramos MJ.
2015.
Insights into the structural determinants of substrate specificity and activity in mouse aldehyde oxidases. Journal of Biological Inorganic Chemistry. 20:209-217., Number 2
AbstractIn this work, a combination of homology modeling and molecular dynamics (MD) simulations was used to investigate the factors that modulate substrate specificity and activity of the mouse AOX isoforms: mAOX1, mAOX2 (previously mAOX3l1), mAOX3 and mAOX4. The results indicate that the AOX isoform structures are highly preserved and even more conserved than the corresponding amino acid sequences. The only differences are at the protein surface and substrate-binding site region. The substrate-binding site of all isoforms consists of two regions: the active site, which is highly conserved among all isoforms, and a isoform-specific region located above. We predict that mAOX1 accepts a broader range of substrates of different shape, size and nature relative to the other isoforms. In contrast, mAOX4 appears to accept a more restricted range of substrates. Its narrow and hydrophobic binding site indicates that it only accepts small hydrophobic substrates. Although mAOX2 and mAOX3 are very similar to each other, we propose the following pairs of overlapping substrate specificities: mAOX2/mAOX4 and mAOX3/mAXO1. Based on these considerations, we propose that the catalytic activity between all isoforms should be similar but the differences observed in the binding site might influence the substrate specificity of each enzyme. These results also suggest that the presence of several AOX isoforms in mouse allows them to oxidize more efficiently a wider range of substrates. This contrasts with the same or other organisms that only express one isoform and are less efficient or incapable of oxidizing the same type of substrates.
Carvalho, AL, Dias FMV, Nagy T, Prates JAM, Proctor MR, Smith N, Bayer EA, Davies GJ, Ferreira LMA, Romao MJ, Fontes CMGA, Gilbert HJ.
2007.
Evidence for a dual binding mode of dockerin modules to cohesins. Proceedings of the National Academy of Sciences of the United States of America. 104:3089-3094., Number 9
Abstractn/a
Carvalho, AL, Goyal A, Prates JAM, Bolam DN, Gilbert HJ, Pires VMR, Ferreira LMA, Planas A, Romao MJ, Fontes C.
2004.
The family 11 carbohydrate-binding module of Clostridium thermocellum Lic26A-Cel5E accommodates beta-1,4- and beta-1,3-1,4-mixed linked glucans at a single binding site. Journal of Biological Chemistry. 279:34785-34793., Number 33
Abstractn/a
Carvalho, AL, Pires VMR, Gloster TM, Turkenburg JP, Prates JAM, Ferreira LMA, Romao MJ, Davies GJ, Fontes C, Gilbert HJ.
2005.
Insights into the structural determinants of cohesin dockerin specificity revealed by the crystal structure of the type II cohesin from Clostridium thermocellum SdbA. Journal of Molecular Biology. 349:909-915., Number 5
Abstractn/a
Carvalho, AL, Dias FMV, Prates JAM, Nagy T, Gilbert HJ, Davies GJ, Ferreira LMA, Romao MJ, Fontes C.
2003.
Cellulosome assembly revealed by the crystal structure of the cohesin-dockerin complex. Proceedings of the National Academy of Sciences of the United States of America. 100:13809-13814., Number 24
Abstractn/a
Carvalho, AL, Santos-Silva T, Romão MJ, Eurico J, Marcelo F.
2018.
{CHAPTER 2 Structural Elucidation of Macromolecules}, sep. Essential Techniques for Medical and Life Scientists: A Guide to Contemporary Methods and Current Applications with the Protocols. :30–91.: BENTHAM SCIENCE PUBLISHERS
Abstractn/a