메뉴 건너뛰기




Volumn 89, Issue C, 1982, Pages 108-121

Synthesis of Ribulose 1,5-Bisphosphate: Routes from Glucose 6-Phosphate (Via 6-Phosphogluconate) and from Adenosine Monophosphate (via Ribose 5-Phosphate)

Author keywords

[No Author keywords available]

Indexed keywords

6 PHOSPHOGLUCONIC ACID; 6-PHOSPHOGLUCONATE; ADENOSINE PHOSPHATE; GLUCONIC ACID; GLUCOSE; GLUCOSE 6 PHOSPHATE; GLUCOSE PHOSPHATE; PENTOSE PHOSPHATE; RIBOSE 5 PHOSPHATE; RIBOSE PHOSPHATE; RIBOSE-5-PHOSPHATE; RIBULOSE 1,5 DIPHOSPHATE; RIBULOSE PHOSPHATE; RIBULOSE-1,5 DIPHOSPHATE; XYLULOSE 1,5 BISPHOSPHATE; XYLULOSE 1,5-BISPHOSPHATE;

EID: 0020430517     PISSN: 00766879     EISSN: 15577988     Source Type: Book Series    
DOI: 10.1016/S0076-6879(82)89020-4     Document Type: Article
Times cited : (27)

References (23)
  • 2
    • 0019877105 scopus 로고
    • Active RuBPC is a ternary complex (ECM) composed of enzyme (E), CO2(C), and Mg2+ (M). This complex is in equilibrium with an inactive form of the enzyme, and the interconversion of these forms is slow. XuBP combines very tightly with the inactive enzyme and acts as a noncompetitive inhibitor. It also binds less tightly to the ECM form of the enzyme as a competitive inhibitor.
    • McCurry, S.D., Pierce, J., Tolbert, N.E., Orme-Johnson, W.H., J. Biol. Chem., 256, 1981, 6623 Active RuBPC is a ternary complex (ECM) composed of enzyme (E), CO2(C), and Mg2+ (M). This complex is in equilibrium with an inactive form of the enzyme, and the interconversion of these forms is slow. XuBP combines very tightly with the inactive enzyme and acts as a noncompetitive inhibitor. It also binds less tightly to the ECM form of the enzyme as a competitive inhibitor.
    • (1981) J. Biol. Chem. , vol.256 , pp. 6623
    • McCurry, S.D.1    Pierce, J.2    Tolbert, N.E.3    Orme-Johnson, W.H.4
  • 4
  • 5
    • 0017886089 scopus 로고
    • The rate of degradation of RuBP at pH 8.3 and 30° was 1.25% per hour. We determined the stability of RuBP (0.5 m M, in 0.1 M Tris, pH 8.0, 30°) in solution by measuring the concentration of RuBP with the coupled enzymic method. The observed half-life for RuBP was 48 hr.
    • Paech, C., Pierce, J., McCurry, S.D., Tolbert, N.E., Biochem. Biophys. Res. Commun., 83, 1978, 1084 The rate of degradation of RuBP at pH 8.3 and 30° was 1.25% per hour. We determined the stability of RuBP (0.5 m M, in 0.1 M Tris, pH 8.0, 30°) in solution by measuring the concentration of RuBP with the coupled enzymic method. The observed half-life for RuBP was 48 hr.
    • (1978) Biochem. Biophys. Res. Commun. , vol.83 , pp. 1084
    • Paech, C.1    Pierce, J.2    McCurry, S.D.3    Tolbert, N.E.4
  • 16
    • 85012600289 scopus 로고    scopus 로고
    • this series
    • E. Racker, this series, Vol. 5, p. 266.
    • , vol.5 , pp. 266
    • Racker, E.1
  • 20
    • 85012800219 scopus 로고    scopus 로고
    • this series
    • B. L. Horecker, this series, Vol. 3, p. 105.
    • , vol.3 , pp. 105
    • Horecker, B.L.1
  • 21


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.