Zobrazeno 1 - 10
of 23
pro vyhledávání: '"Shinichi Taoka"'
Autor:
Ian Henderson, Ardis Barthuli, Jayanta Sinha, Sarah A. Fanders, Mark A. Gouthro, John T. Ross, Michael M. Meagher, Theresa J. Smith, Mehmet Inan, Leonard A. Smith, Rick Barent, Bonnie M. Loveless, Todd Swanson, Shinichi Taoka
Publikováno v:
Journal of Biotechnology. 127:462-474
A process was developed for production of a candidate vaccine antigen, recombinant C-terminal heavy chain fragment of the botulinum neurotoxin serotype E, rBoNTE(H(c)) in Pichia pastoris. P. pastoris strain GS115 was transformed with the rBoNTE(H(c))
Autor:
John T. Groves, Thomas G. Spiro, Colin L. Weeks, Steen Brøndsted Nielsen, Shinichi Taoka, Mrinalini Puranik, Omer Kabil, Dorothee Lahaye, Ruma Banerjee
Publikováno v:
Journal of Biological Chemistry. 281:13433-13438
Cystathionine beta-synthase (CBS) condenses homocysteine, a toxic metabolite, with serine in a pyridoxal phosphate-dependent reaction. It also contains a heme cofactor to which carbon monoxide (CO) or nitric oxide can bind, resulting in enzyme inhibi
Autor:
Shinichi Taoka, Ruma Banerjee
Publikováno v:
Journal of Biological Chemistry. 277:22421-22425
Cystathionine beta-synthase found in yeast catalyzes a pyridoxal phosphate-dependent condensation of homocysteine and serine to form cystathionine. Unlike the homologous mammalian enzymes, yeast cystathionine beta-synthase lacks a second cofactor, he
Publikováno v:
Journal of Inorganic Biochemistry. 87:253-259
Cystathionine beta-synthase is a key heme and pyridoxal phosphate-dependent enzyme involved in homocysteine metabolism in humans. The role of the recently discovered heme in this protein remains an important open question. The axial ligands to the he
Autor:
Shinichi Taoka, Ruma Banerjee
Publikováno v:
Journal of Inorganic Biochemistry. 87:245-251
Homocysteine is a key junction metabolite that can be converted to cystathionine in a reaction catalyzed by the heme and pyridoxal phosphate-dependent cystathionine beta-synthase. The heme has unusual spectroscopic properties and the axial ligands ha
Publikováno v:
Biochemistry. 40:459-463
Human cystathionine beta-synthase (CBS) is an essential enzyme for the removal of the toxic metabolite homocysteine. Heme and pyridoxal phosphate (PLP) cofactors are necessary to catalyze the condensation of homocysteine and serine to generate cystat
Publikováno v:
Biochemistry. 38:13155-13161
Cystathionine beta-synthase is a unique heme protein that catalyzes a pyridoxal phosphate (or PLP)-dependent beta-replacement reaction. The reaction involves the condensation of serine and homocysteine and constitutes one of the two major avenues for
Autor:
James M. Puckett, Huilan Chen, Ruma Banerjee, Laibin Luo, Craig L. Semerad, Luigi G. Marzilli, Antonia M. Calafat, Hon Yan, Shinichi Taoka
Publikováno v:
Biochemistry. 34:14125-14130
The cofactor analog 2',5'-dideoxyadenosylcobalamin (ddAdoCbl) differs from the natural cofactor coenzyme B12 [5'-deoxyadenosylcobalamin (dAdoCbl)] by lacking only one oxygen atom. The 1H and 13C NMR spectra of ddAdoCbl have been assigned unambiguousl
Publikováno v:
Journal of Biological Chemistry. 269:31630-31634
Human methylmalonyl-CoA mutase is inhibited by ethylmalonyl-CoA, cyclopropylcarbonyl-CoA carboxylate, and methylenecyclopropylacetyl-CoA, which are substrate, intermediate, and product analogs, respectively. The mode of inhibition by each analog is r
Publikováno v:
Journal of Biological Chemistry. 269:17988-17992
The catalysis of the hydration of CO2 by human carbonic anhydrase II (HCA II) includes the transfer of a proton from zinc-bound water to histidine 64 utilizing a network of intervening hydrogen-bonded water molecules, then the proton is transferred t