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1 eactions with both tyrosine phenol-lyase and tryptophan indole-lyase.
2 quinonoid intermediate in its reaction with tryptophan indole-lyase.
3 es (kcat < 1% of L-trp) for Escherichia coli tryptophan indole-lyase.
4 r to tryptophan in its reaction with E. coli tryptophan indole-lyase.
5 erved in sequences of TPL and the paralogue, tryptophan indole-lyase.
6 onoid intermediates formed both by wild-type tryptophan indole-lyase and by wild type and Y71F tyrosi
7 and inhibitors to wild-type Proteus vulgaris tryptophan indole-lyase and to wild type and Y71F Citrob
8 ted tyrosines with tyrosine phenol-lyase and tryptophan indole-lyase are due to a combination of ster
10 ion of benzimidazole and l-Trp or l-Ser with tryptophan indole-lyase crystals does not result in the
13 quinonoid intermediates in the reaction with tryptophan indole-lyase; however, 6,7-thiatryptophan is
14 ter substrate (kcat/K(m) = 32% of L-trp) for tryptophan indole-lyase than is 4,5-thiatryptophan (kcat
18 F and H463F mutant forms of Escherichia coli tryptophan indole-lyase (Trpase) have been prepared.
21 s of tyrosine with tyrosine phenol-lyase and tryptophan indole-lyase (tryptophanase) were studied by
22 quinonoid intermediates in the reaction with tryptophan indole-lyase, whereas 4-aza- and 5-azatryptop
23 for tryptophan indole-lyase; the reaction of tryptophan indole-lyase with L-tyrosine resulted in form
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