Literature DB >> 24178640

Tryptophanase-catalysed degradation of D-tryptophan in highly concentrated diammonium hydrogen phosphate solution.

A Shimada1, H Shishido, I Nakamura.   

Abstract

Tryptophanase is and is perfectly inert to D-tryptophan under ordinary conditions. However, activity that can degrade D-tryptophan into indole is observed when tryptophanase is in highly concentrated diammoniumhydrogen phosphate solution. The reaction has been so far unknown in tryptophanase metabolic pathways. Here we report the characteristic of the reaction. We also discuss its significance in relation to selection of an amino acid optical isomer from a racemic mixture.

Entities:  

Year:  1996        PMID： 24178640     DOI： 10.1007/BF00805723

Source DB:  PubMed          Journal:  Amino Acids        ISSN： 0939-4451            Impact factor:   3.520


  9 in total

1.  Equilibria and absorption spectra of tryptophanase.

Authors:  C M Metzler; R Viswanath; D E Metzler
Journal:  J Biol Chem       Date:  1991-05-25       Impact factor: 5.157

Review 2.  Tryptophanase: structure, catalytic activities, and mechanism of action.

Authors:  E E Snell
Journal:  Adv Enzymol Relat Areas Mol Biol       Date:  1975

3.  Tryptophanase from Escherichia coli B/1t7-A.

Authors:  I Behbahani-Nejad; J L Dye; C H Suelter
Journal:  Methods Enzymol       Date:  1987       Impact factor: 1.600

4.  The folding characteristics of tryptophanase from Escherichia coli.

Authors:  T Mizobata; Y Kawata
Journal:  J Biochem       Date:  1995-02       Impact factor: 3.387

5.  In vitro protein synthesis using D-amino acids and its evolutionary significance.

Authors:  M Isoyama; H Ohoka; H Kikuchi; A Shimada; S Yuasa
Journal:  Orig Life       Date:  1984

6.  Resolution of amino acids by a native-cellulose column.

Authors:  S Yuasa; M Itoh; A Shimada
Journal:  J Chromatogr Sci       Date:  1984-07       Impact factor: 1.618

7.  Prevention of amino acid racemization during guanidination--a prerequisite for measurement of protein digestibility by homoarginine labeling.

Authors:  M de Vrese; K Middendorf; H Hagemeister
Journal:  Z Ernahrungswiss       Date:  1994-12

8.  The pH-dependent behavior of catalytic activities of Azospirillum brasilense glutamate synthase and iodoacetamide modification of the enzyme provide evidence for a catalytic Cys-His ion pair.

Authors:  M A Vanoni; P Accornero; G Carrera; B Curti
Journal:  Arch Biochem Biophys       Date:  1994-03       Impact factor: 4.013

9.  Evolutionary relationships among pyridoxal-5'-phosphate-dependent enzymes. Regio-specific alpha, beta and gamma families.

Authors:  F W Alexander; E Sandmeier; P K Mehta; P Christen
Journal:  Eur J Biochem       Date:  1994-02-01
  9 in total
  2 in total

1.  Structure of Escherichia coli tryptophanase purified from an alkaline-stressed bacterial culture.

Authors:  Stephane Rety; Patrick Deschamps; Nicolas Leulliot
Journal:  Acta Crystallogr F Struct Biol Commun       Date:  2015-10-23       Impact factor: 1.056

2.  Tryptophanase-catalyzed L-tryptophan synthesis from D-serine in the presence of diammonium hydrogen phosphate.

Authors:  Akihiko Shimada; Haruka Ozaki; Takeshi Saito; Fujii Noriko
Journal:  Int J Mol Sci       Date:  2009-06-03       Impact factor: 6.208
  2 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.