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Tryptophan synthase
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S-Phenyl-L-cysteine is regarded as having potential applicability as an antiretroviral/protease inhibitor for human immunodeficiency virus (HIV). In the present study, optically active S-phenyl-L-cysteine was prepared in a highly efficient manner from inexpensive bromobenzene using tryptophan synthase through a chemoenzymatic method.
8p
vihamax2711
21-04-2020
16
0
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The amino acid residue tryptophan 27 of 6,7-dimethyl-8-ribityllumazine synthase of the yeastSchizosaccharomyces pombewas replacedby tyrosine. The structures of theW27Y mutant protein in complex with riboflavin, the substrate analogue 5-nitroso-6-ribitylamino-2,4(1H,3H)-pyrimidin-edione, and the product analogue 6-carboxyethyl-7-oxo-8-ribityllumazine,weredeterminedbyX-raycrystallography at resolutions of 2.7–2.8 A ˚ .
7p
awards
05-04-2013
41
4
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The structure of the tryptophan synthaseb2 subunit (Pfb2 ) from the hyperthermophile,Pyrococcus furiosus,was deter-mined by X-ray crystallographic analysis at 2.2 A˚ resolu-tion, and its stability was examined byDSC. This is the first report of the X-ray structure of the tryptophan synthaseb2 subunit alone, although the structure of the tryptophan synthase a2b2 complex fromSalmonella typhimuriumhas already been reported. The structure ofPfb2was essentially similartothatoftheb2 subunit (Stb2)inthea2b2complex from S. typhimurium....
12p
dell39
03-04-2013
50
3
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In rat neuronal nitric oxide synthase, Phe1395 is positioned over the FAD isoalloxazine ring. This is replaced by Trp676 in human cytochrome P450 reductase, a tryptophan in related diflavin reductases (e.g. methionine synthase reduc-tase andnovel reductase 1), and tyrosine inplant ferredoxin-NADP + reductase. Trp676 in human cytochrome P450 reductase is conformationallymobile, andplays akey role in enzyme reduction. Mutagenesis of Trp676 to alanine results in a functional NADH-dependent reductase. ...
13p
dell39
03-04-2013
35
3
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Tuberculosis (TB) continues to be a major cause of morbidity and mortal-ity worldwide. The increasing emergence and spread of drug-resistant TB poses a significant threat to disease control and calls for the urgent devel-opment of new drugs. The tryptophan biosynthetic pathway plays an important role in the survival of Mycobacterium tuberculosis.
11p
vinaphone15
27-02-2013
45
1
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To understand the basis for the lower activity of the tryptophan synthaseb2 subunit in comparison to thea2b2 complex, we determined the crystal struc-tures of apo-b2 and holo-b2 from Escherichia coliat 3.0 and 2.9 A˚ resolu-tions, respectively. To our knowledge, this is the first report of both b2 subunit structures with and without pyridoxal-5¢-phosphate.
14p
mobifone23
21-01-2013
47
3
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Tuyển tập báo cáo các nghiên cứu khoa học quốc tế ngành y học dành cho các bạn tham khảo đề tài: Characterisation of the tryptophan synthase alpha subunit in maize
11p
panasonic06
26-12-2011
47
3
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