R Contestabile

Summary

Affiliation: University of Rome La Sapienza
Country: Italy

Publications

  1. pmc Asymmetry of the active site loop conformation between subunits of glutamate-1-semialdehyde aminomutase in solution
    Barbara Campanini
    Dipartimento di Farmacia, Universita di Parma, Parco Area delle Scienze 23 A, 43124 Parma, Italy
    Biomed Res Int 2013:353270. 2013
  2. ncbi request reprint l-Threonine aldolase, serine hydroxymethyltransferase and fungal alanine racemase. A subgroup of strictly related enzymes specialized for different functions
    R Contestabile
    Dipartimento di Scienze Biochimiche A Rossi Fanelli and Centro di Biologia Molecolare del Consiglio Nazionale delle Ricerche, Universita degli Studi di Roma, La Sapienza, Roma, Italy
    Eur J Biochem 268:6508-25. 2001
  3. ncbi request reprint Role of tyrosine 65 in the mechanism of serine hydroxymethyltransferase
    R Contestabile
    Dipartimento di Scienze Biochimiche A Rossi Fanelli and Centro di Biologia Molecolare del Consiglio Nazionale delle Ricerche, Universita La Sapienza, Roma, Italy
    Biochemistry 39:7492-500. 2000

Collaborators

Detail Information

Publications3

  1. pmc Asymmetry of the active site loop conformation between subunits of glutamate-1-semialdehyde aminomutase in solution
    Barbara Campanini
    Dipartimento di Farmacia, Universita di Parma, Parco Area delle Scienze 23 A, 43124 Parma, Italy
    Biomed Res Int 2013:353270. 2013
    ..Iodide induces release of the cofactor from PMP-GSAM, apparently from only one catalytic site, therefore suggesting an asymmetry also in this form of the enzyme in solution, in contrast with the crystallographic data. ..
  2. ncbi request reprint l-Threonine aldolase, serine hydroxymethyltransferase and fungal alanine racemase. A subgroup of strictly related enzymes specialized for different functions
    R Contestabile
    Dipartimento di Scienze Biochimiche A Rossi Fanelli and Centro di Biologia Molecolare del Consiglio Nazionale delle Ricerche, Universita degli Studi di Roma, La Sapienza, Roma, Italy
    Eur J Biochem 268:6508-25. 2001
    ..coli and alanine racemase from Cochliobolus carbonum, and their comparison with the SHMT crystal structure, indicated how the tetrahydrofolate binding site might have evolved and offered a starting point for further investigations...
  3. ncbi request reprint Role of tyrosine 65 in the mechanism of serine hydroxymethyltransferase
    R Contestabile
    Dipartimento di Scienze Biochimiche A Rossi Fanelli and Centro di Biologia Molecolare del Consiglio Nazionale delle Ricerche, Universita La Sapienza, Roma, Italy
    Biochemistry 39:7492-500. 2000
    ..These data are consistent with a role for the Tyr65 hydroxyl group in the conversion of a closed active site to an open structure...