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<< < Results 11 - 20 of 22 > >>
EC Number Protein Variants Commentary Reference
Show all pathways known for 3.7.1.3Display the word mapDisplay the reaction diagram Show all sequences 3.7.1.3D201E mutation results in reduced catalytic activity with L-kynurenine and beta-benzoyl-L-alanine, but not O-benzoyl-L-serine. The mutant enzyme can form quinonoid and vinylogous amide intermediates with beta-benzoyl-L-alanine, similar to wild-type enzyme. The mutant enzyme reacts more slowly with beta-benzoyl-L-alanine and benzaldehyde to form an aldol product absorbing at 490 nm than wild-type 756117
Show all pathways known for 3.7.1.3Display the word mapDisplay the reaction diagram Show all sequences 3.7.1.3H102W/N333T the mutant shows complete reversal of substrate specificity between 3-hydroxy-L-kynurenine and L-kynurenine 699466
Show all pathways known for 3.7.1.3Display the word mapDisplay the reaction diagram Show all sequences 3.7.1.3H102W/S332G/N333T the mutant shows complete reversal of substrate specificity between 3-hydroxy-L-kynurenine and L-kynurenine 699466
Show all pathways known for 3.7.1.3Display the word mapDisplay the reaction diagram Show all sequences 3.7.1.3more cosmid pRA3 corrects trpA mutants of Rhizobium leguminosarum 673365
Show all pathways known for 3.7.1.3Display the word mapDisplay the reaction diagram Show all sequences 3.7.1.3more cosmid pRA3 corrects trpA, trpB and trpC mutants in Escherichia coli 673365
Show all pathways known for 3.7.1.3Display the word mapDisplay the reaction diagram Show all sequences 3.7.1.3N333T the mutant reveals a 9fold decrease in kcat for L-kynurenine, but no change in Km, the mutant has weaker 3-hydroxy-L-kyrenine binding (6fold higher Km) and kcat at least 1100times slower than wild type Kynase 699466
Show all pathways known for 3.7.1.3Display the word mapDisplay the reaction diagram Show all sequences 3.7.1.3S332G/N333T the mutant shows a very slight preference for L-kynurenine over 3-hydroxy-L-kynurenine 699466
Show all pathways known for 3.7.1.3Display the word mapDisplay the reaction diagram Show all sequences 3.7.1.3S36A the mutant enzyme can form quinonoid and vinylogous amide intermediates with beta-benzoyl-L-alanine, similar to wild-type enzyme. Mutation results in a 230fold reduction of kcat and 30fold reduction in kcat/Km with L-kynurenine, but very little effect on the reaction of O-benzoyl-L-serine. The rate-determining step in the reaction of thje mutant enzyme the Cbeta-Cgamma bond cleavage 756117
Show all pathways known for 3.7.1.3Display the word mapDisplay the reaction diagram Show all sequences 3.7.1.3T102I the mutation leads to a marked decrease in kynureninase activity and causes the red body coloration in the Bombyx mori red blood strain 698102
Show all pathways known for 3.7.1.3Display the word mapDisplay the reaction diagram Show all sequences 3.7.1.3T198A screening of cDNA from KYNU revealed homozygosity for a c.593A>G substitution in exon 7 in the proband, leading to a threonine-to-alanine shift, T198A, in kynureninase 688175
<< < Results 11 - 20 of 22 > >>