Tryptophanase and

Table 9.2 1 The dissymmetry factor and reduced linear dichroism values in the coenzyme absorption bands of tryptophanase and its complexes with inhibitory amino acidst2...

Several monovalent cations (NH4+, K+, Tl+, Rb+) have been shown to activate tryptophanase and increase its affinity for PLP.2,37,59 The cations also strongly affect the... 

Incubation in solutions of low denaturant concentration can sometimes cause inactivation. Formation of an incorrectly folded form of human carbonic anhydrase in 1.7M GuHCl which subsequently aggregates has been documented (77). Other proteins have also been observed to improperly refold at relatively low concentrations of denaturant These proteins include 6-galactosidase, tryptophanase, and elastase (6). 

Cystathionase also has a low level of direct cysteine desulphydrase activity. Tryptophanase and tryptophan synthetase are other enzymes capable of carrying out the cysteine desulphydrase reaction. Such considerations have cast doubt on this biological significance of this reaction, although strong arguments have been presented for a true cysteine desulphydrase in SalmonellcP. 

Studies of the recycling of the cofactor in an enzyme reactor comparison of reactions using free or immobilized nicotinamide adenine dinucleotide Investigations of the role of carbonic anhydrases in vivo Purification of tryptophanase and tyrosine phenol-lyase... 

Fig. 23. Mechanism of reaction of tryptophanase and tryptophan synthase. Reprinted from Reference 43 with permission of the American Chemical Society.

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