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PLP1  -  proteolipid protein 1

Gallus gallus

 
 
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Disease relevance of PLP1

  • The substrate-free Escherichia coli tyrosine aminotransferase (eTAT) bound with the cofactor pyridoxal 5'-phosphate (PLP) was crystallized in the trigonal space group P3(2) [1].
 

High impact information on PLP1

 

Anatomical context of PLP1

  • The addition of PLP in vitro enhanced the catalytic activity of the plasma enzyme, but had negligible effect on the erythrocyte enzyme [3].

References

  1. Crystallization and preliminary crystallographic analysis of the Escherichia coli tyrosine aminotransferase. Ko, T.P., Wu, S.P., Yang, W.Z., Tsai, H., Yuan, H.S. Acta Crystallogr. D Biol. Crystallogr. (1999) [Pubmed]
  2. Characterization of the estrogen receptor extracted from hen oviduct nuclei with pyridoxal phosphate. Seeley, D.H., Mester, J., Baulieu, E.E., Wolfson, A.J. Endocrinology (1984) [Pubmed]
  3. Aspartate aminotransferase activity in experimentally induced asymptomatic vitamin B6 deficiency in chicks. Massé, P.G., Vuilleumier, J.P., Weiser, H. Ann. Nutr. Metab. (1991) [Pubmed]
  4. Progesterone down-regulation of nuclear estrogen receptor: a fundamental mechanism in birds and mammals. Selcer, K.W., Leavitt, W.W. Gen. Comp. Endocrinol. (1988) [Pubmed]
  5. Modification of skeletal S-1 with fluorescein isothiocyanate. López-Zabalza, M.J., Sanz, S., Iriarte, A., López-Moratalla, N., Santiago, E. Comp. Biochem. Physiol., B (1990) [Pubmed]
 
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