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Last Updated: 2 years ago

Possible Interaction: Alanine and Arginine

supplement:

Alanine

supplement:

Arginine

Research Papers that Mention the Interaction

Substitution of the arginine residues with alanines resulted in the loss of these properties.
Journal of Biological Chemistry  •  2004  |  View Paper
Replacement … the P1 arginine … alanine led to the complete suppression of processing, as occurs also in a naturally occurring serine mutation at this site (Yoshimasa, Y., Seino, …., Whittaker, J., Kakehi, T., Kosaki, A., Kuzuya, H., Imura, H., Bell, G. I., and Steiner, D. F. (1988) Science 240, 783-787).
The Journal of biological chemistry  •  1990  |  View Paper
Substitution of this arginine with an alanine induced changes in thermal stability and/or intrinsic fluorescence of the related HspB1 and HspB8, but yielded only modest changes in the same biophysical properties of HspB4, HspB5, and HspB6 which together belong to another clade of vertebrate sHsps.
International journal of molecular sciences  •  2018  |  View Paper
Mutation analyses revealed that stepwise substitution of arginine residues within the CBD1 (amino acids 40–54) and CBD2 (amino acids 328–377) regions with alanines progressively impaired chromosome binding activity of EBNA1.
The Journal of Biological Chemistry  •  2013  |  View Paper
Arginine led to significant increases in PMN arginine, ornithine, citrulline, aspartate, glutamate and alanine concentrations as well as increased H2O2-generation and MPO activity while O2−-formation was decreased.
Amino Acids  •  2002  |  View Paper
Inhibition was lost when either arginine was substituted with alanine.
Journal of immunology  •  1999  |  View Paper
Net utilization of lysine, threonine, isoleucine, leucine, glycine and alanine by jejunal or ileal mixed bacteria decreased (P < 0.05) with the addition of arginine.
Amino Acids  •  2011  |  View Paper
Conversion of each of these residues to alanine resulted in strong increases in Km and decreases in kcat values for pyruvate and l‐arginine , but had little effect on the Km and kcat values for NADH.
The FEBS journal  •  2007  |  View Paper
Substitution of the arginine at position 7 of PA224 with an alanine reduced the accessible side chains of the epitope.
Nature Immunology  •  2005  |  View Paper
On the other hand, impairment of NO from Arginine driven by ALA , although not modulating in vitro the ALA-PDT response, by increasing in vivo blood flow, may be contributing to the mechanism of tumour cures.
Two unexpected results were found: the enhancement of NO production from the donor sodium nitroprusside (SNP) induced by ALA in both cells and medium, and the inhibition by ALA of NO production from arginine.
Journal of photochemistry and photobiology. B, Biology  •  2005  |  View Paper
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