Taurine and Kynureninase View Full Text


Ontology type: schema:Chapter     


Chapter Info

DATE

1996

AUTHORS

Y. Shibata , T. Ohta , M. Nakatsuka , H. Ishizu , Y. Matsuda , T. Shindo , F. Takeuchi , M. Yoshino , S. Hirano , T. Noguchi

ABSTRACT

Kynureninase is the most important enzyme in tryptophan metabolism. In the main pathway of tryptophan metabolism, kynureninase forms 3-OH-anthranilic acid from 3-OH-kynurenine. In this reaction vitamin B6 is a co-enzyme. An important relationship between -SH groups and liver kynureninase apoenzyme has been reported by Takeuchi8, 9 and Izuta1. We have experimented on kynureninase and S-involved compounds as follows: (i) Kynureninase activity was inhibited in vitamin B6-deficient rats and in streptozotocin (STZ)-induced diabetic rats; (ii) Following tryptophan administration, in rats given taurine or oysters (rich in taurine), the excretion of xanthurenic acid (an index of vitamin B6 deficiency) decreased compared with an excess methionine-administered group; and (iii) The active center of kynureninase apoenzyme (464 amino acid residues) is located near cysteine. More... »

PAGES

55-58

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/978-1-4899-0182-8_6

DOI

http://dx.doi.org/10.1007/978-1-4899-0182-8_6

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1050553578

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/8915341


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