메뉴 건너뛰기




Volumn 73, Issue 23, 2008, Pages 9314-9319

Theoretical studies of the quinolinic acid to nicotinic acid mononucleotide transformation

Author keywords

[No Author keywords available]

Indexed keywords

ACIDS; AMIDES; BIOCHEMICAL ENGINEERING; BIOCHEMISTRY; CHEMICAL REACTIONS; ENZYMES; MATHEMATICAL TRANSFORMATIONS; PYRIDINE;

EID: 57449086148     PISSN: 00223263     EISSN: None     Source Type: Journal    
DOI: 10.1021/jo8012379     Document Type: Article
Times cited : (2)

References (72)
  • 6
    • 0343770631 scopus 로고
    • Everse, J, Anderson, B, You, K. S, Eds, Academic Press: New York
    • White, H. B. In Pyridine Coenzyme Nucleotides; Everse, J., Anderson, B., You, K. S., Eds.; Academic Press: New York, 1982; pp 1-17.
    • (1982) Pyridine Coenzyme Nucleotides , pp. 1-17
    • White, H.B.1
  • 17
    • 0036334571 scopus 로고    scopus 로고
    • Gerdes, S. Y.; et al. J. Bacterial. 2002, 184, 4555-4572.
    • (2002) J. Bacterial , vol.184 , pp. 4555-4572
    • Gerdes, S.Y.1
  • 19
    • 0026539659 scopus 로고    scopus 로고
    • Heyes, M. P.; Saito, K.; Crowley, J. S.; David, L. E.; Demitrack, M. A.; Der, M.; Dilling, L. A.; Elia, J.; Kruesi, M. J.; Lackner, A. Brain 1992, 115, 1249-1273.
    • Heyes, M. P.; Saito, K.; Crowley, J. S.; David, L. E.; Demitrack, M. A.; Der, M.; Dilling, L. A.; Elia, J.; Kruesi, M. J.; Lackner, A. Brain 1992, 115, 1249-1273.
  • 24
  • 25
    • 84925570382 scopus 로고    scopus 로고
    • Orotidine Monophosphate Decarboxylase: A Mechanistic Dialogue; Topics in Current Chemistry; Lee, J. K., Tantillo, D. J., Eds. Springer: Berlin, 2004; 238. and references therein.
    • Orotidine Monophosphate Decarboxylase: A Mechanistic Dialogue; Topics in Current Chemistry; Lee, J. K., Tantillo, D. J., Eds. Springer: Berlin, 2004; Vol. 238. and references therein.
  • 27
    • 0028918401 scopus 로고
    • and references therein
    • Radzicka, A.; Wolfenden, R. Science 1995, 267, 90-93, and references therein.
    • (1995) Science , vol.267 , pp. 90-93
    • Radzicka, A.1    Wolfenden, R.2
  • 36
    • 84925560741 scopus 로고    scopus 로고
    • 2+ in our calculations.
    • 2+ in our calculations.
  • 40
    • 84925564087 scopus 로고    scopus 로고
    • Another mechanistic possibility is the protonation of QA at N1, which would induce C2 decarboxylation. Proton transfer from N1 to C2 would be followed by alkylation. We did not explore this path as it is not suggested in the biochemical literature, but it is a logical possibility
    • Another mechanistic possibility is the protonation of QA at N1, which would induce C2 decarboxylation. Proton transfer from N1 to C2 would be followed by alkylation. We did not explore this path as it is not suggested in the biochemical literature, but it is a logical possibility.
  • 46
    • 84925564086 scopus 로고    scopus 로고
    • For orotate phosphoribosyl transferase, although inversion of stereochemistry is observed, kinetic isotope effects do imply a transition state with much oxycarbonium character.41
    • 41
  • 50
    • 84925564085 scopus 로고    scopus 로고
    • To properly consider solvation and enzyme site binding, specific interactions need to be considered; computationally this would involve QM/MM calculations, which would be the topic of a future study. For discussion on QM/MM methods see: Warshel, A. Computer Modeling of Chemical Reactions in Enzymes and Solutions; John Wiley and Sons: New York, 1991.
    • To properly consider solvation and enzyme site binding, specific interactions need to be considered; computationally this would involve QM/MM calculations, which would be the topic of a future study. For discussion on QM/MM methods see: Warshel, A. Computer Modeling of Chemical Reactions in Enzymes and Solutions; John Wiley and Sons: New York, 1991.
  • 51
    • 84925570381 scopus 로고    scopus 로고
    • We did not calculate the carboxylate-ammonium complexes in water since the complex itself is already hydrogen-bound and is designed to very roughly mimic the enzyme active site
    • We did not calculate the carboxylate-ammonium complexes in water since the complex itself is already hydrogen-bound and is designed to very roughly mimic the enzyme active site.
  • 52
    • 84925564084 scopus 로고    scopus 로고
    • The gas phase decarboxylations of 2, 3, 6, and 7 were also calculated at MP2/6-31+G*/B3LYP/6-31+G*; values are consistent with the B3LYP/6-31+G* calculations (data in Supporting Information).
    • The gas phase decarboxylations of 2, 3, 6, and 7 were also calculated at MP2/6-31+G*/B3LYP/6-31+G*; values are consistent with the B3LYP/6-31+G* calculations (data in Supporting Information).
  • 53
    • 84925567198 scopus 로고    scopus 로고
    • 48
    • 48
  • 59
    • 84925560740 scopus 로고    scopus 로고
    • 56
    • 56
  • 72
    • 84925570380 scopus 로고    scopus 로고
    • The vinylic anion formed from decarboxylation is quite basic and proton transfer probably will occur quickly; it is also possible that the two steps will occur in concert
    • The vinylic anion formed from decarboxylation is quite basic and proton transfer probably will occur quickly; it is also possible that the two steps will occur in concert.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.