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Your search keyword '"Scott AI"' showing total 14 results
Start Over Author "Scott AI" Topic chemistry.chemical_compound
14 results on '"Scott AI"'

4. Sirohydrochlorin. Prosthetic group of a sulfite reductase enzyme and its role in the biosynthesis of vitamin B12

Author

Anthony J. Irwin, Schoolery Jn, Scott Ai, and Lewis M. Siegel

Subjects
chemistry.chemical_classification, Porphyrins, biology, General Chemistry, Reductase, Uroporphyrins, Biochemistry, Catalysis, Sulfite reductase, Cofactor, Vitamin B 12, chemistry.chemical_compound, Colloid and Surface Chemistry, Enzyme, chemistry, Biosynthesis, biology.protein, Sulfites, Vitamin B12, Oxidoreductases, Sirohydrochlorin
Published
1978

5. Carbon-13 Fourier transform NMR. VII. Stereochemistry of methyl group insertion in corrinoid biosynthesis. Determination of carbon isotope chirality by carbon-13 nuclear magnetic resonance

Author

Cushley Rj, Craig A. Townsend, and Scott Ai

Subjects
chemistry.chemical_compound, Colloid and Surface Chemistry, Corrinoid, Nuclear magnetic resonance, Biosynthesis, Chemistry, Isotopes of carbon, Stereochemistry, General Chemistry, Chirality (chemistry), Biochemistry, Catalysis, Methyl group
Published
1973

6. Biosynthesis of corrinoids. Uroporphyrinogen III as a precursor of vitamin B12

Author

Okada K, Cushley Rj, Scott Ai, Kajiwara M, and Craig A. Townsend

Subjects
chemistry.chemical_compound, Colloid and Surface Chemistry, Biochemistry, Biosynthesis, Chemistry, Uroporphyrinogen III decarboxylase, Uroporphyrinogen III, General Chemistry, Vitamin B12, Corrinoids, Catalysis
Published
1972

7. The mechansim of action of coenzyme B12. The role thioester in a nonenzyme model reaction for coenzyme B12 Dependent isomerization of methylmalony coenzyme A to succinyl coenzyme A

Author

Scott Ai and Kang K

Subjects
chemistry.chemical_classification, Chemistry, Succinyl coenzyme A synthetase, Coenzyme A, Methylmalonyl-CoA Mutase, General Chemistry, Thioester, Biochemistry, Coenzyme B12, Catalysis, chemistry.chemical_compound, Colloid and Surface Chemistry, Models, Chemical, Cobamides, Succinyl-coenzyme A, Isomerases, Isomerization
Published
1977

8. Purification and properties of strictosidine synthetase (an enzyme condensing tryptamine and secologanin) from Catharanthus roseus cultured cells

Author

Nordlöv H, Lee Sl, Scott Ai, and Mizukami H

Subjects
Tryptamine, Ajmalicine, Strictosidine synthase, biology, Chemistry, Iridoid Glucosides, Catharanthine, Catharanthus roseus, Plants, biology.organism_classification, Biochemistry, Tryptamines, Molecular Weight, chemistry.chemical_compound, Kinetics, Glucosides, Transferases, Strictosidine, Carbon-Nitrogen Lyases, biology.protein, Secologanin, Vinca Alkaloids, Vindoline, Pyrans
Abstract

Strictosidine synthetase, which catalyzes the condensation of tryptamine with secologanin to form strictosidine (isovincoside), was purified 740-fold to homogeneity from cultured cells of Catharanthus roseus in 10% yield. The specific activity is 5.85 nkat/mg. The molecular weight as estimated by gel filtration is 38,000. The isoelectric point is 4.6. Apparent Km values for tryptamine and secologanin are 0.83 and 0.46 mM, respectively. The enzyme shows a broad pH optimum between 5.0 and 7.5. The product of the enzymic reaction is exclusively strictosidine, while no trace of its epimer vincoside can be detected. Sulfhydryl inhibitors have no effect on the enzyme. End products in the biosynthetic pathway of indole alkaloids such as ajmalicine, vindoline, and catharanthine do not inhibit the activity of strictosidine synthetase.

Published
1979

10. Biosynthesis of corrins. A cell-free system from Propionibacterium shermanii

Author

Eun Lee, Yagen B, and Scott Ai

Subjects
S-Adenosylmethionine, Porphyrins, biology, Cell-Free System, Propionibacterium, General Chemistry, biology.organism_classification, Biochemistry, Catalysis, Cell-free system, chemistry.chemical_compound, Vitamin B 12, Colloid and Surface Chemistry, Biosynthesis, chemistry
Published
1973

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