Effects of Nutritional Conditions on Plasmid Stability and Production of Tryptophan Synthase by a RecombinantEscherichia coli

Agricultural and Biological Chemistry ◽

10.1080/00021369.1990.10870027 ◽

1990 ◽

Vol 54 (3) ◽

pp. 619-624 ◽

Author(s):

Toru Matsui ◽

Hiroaki Sato ◽

Seigo Sato ◽

Sukekuni Mukataka ◽

Joji Takahashi

Keyword(s):

Plasmid Stability ◽

Tryptophan Synthase ◽

Nutritional Conditions

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Effects of nutritional conditions on plasmid stability and production of tryptophan synthase by a recombinant Escherichia coli.

Agricultural and Biological Chemistry ◽

10.1271/bbb1961.54.619 ◽

1990 ◽

Vol 54 (3) ◽

pp. 619-624 ◽

Author(s):

Toru MATSUI ◽

Hiroaki SATO ◽

Seigo SATO ◽

Sukekuni MUKATAKA ◽

Joji TAKAHASHI

Keyword(s):

Escherichia Coli ◽

Plasmid Stability ◽

Recombinant Escherichia Coli ◽

Tryptophan Synthase ◽

Nutritional Conditions

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Faculty Opinions recommendation of A small-molecule allosteric inhibitor of Mycobacterium tuberculosis tryptophan synthase.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.727772309.793534094 ◽

2017 ◽

Author(s):

Andrea Mozzarelli

Keyword(s):

Mycobacterium Tuberculosis ◽

Small Molecule ◽

Tryptophan Synthase ◽

Allosteric Inhibitor

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Enzymatic Synthesis of L-Tryptophan Catalyzed by Tryptophan Synthase in a Water/Organic Solvent Biphase System

CHINESE JOURNAL OF CATALYSIS (CHINESE VERSION) ◽

10.3724/sp.j.1088.2011.10349 ◽

2014 ◽

Vol 32 (8) ◽

pp. 1405-1410

Author(s):

Lisheng XU ◽

Junzhong LIU ◽

Zhiyuan WANG ◽

Hongjuan ZHANG ◽

Wei LIU ◽

...

Keyword(s):

Organic Solvent ◽

Enzymatic Synthesis ◽

Tryptophan Synthase

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The effect of free amino acids and related compounds on the activity of plant enzymes. I. Effect of DL-threonine, L-proline, γ-aminobutyric acid, L-asparagine and L-cysteine on the activity of tryptophan synthase (4.2.1.20) in living bean leaf (Phaseolus vulgaris L.)

Collection of Czechoslovak Chemical Communications ◽

10.1135/cccc19713323 ◽

1971 ◽

Vol 36 (9) ◽

pp. 3323-3331

Author(s):

M. Štefl ◽

I. Trčka

Keyword(s):

Amino Acids ◽

Phaseolus Vulgaris ◽

Free Amino Acids ◽

Aminobutyric Acid ◽

Tryptophan Synthase ◽

Phaseolus Vulgaris L ◽

Plant Enzymes ◽

Related Compounds

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Isomerization of (3S)-2,3-dihydro-5-fluoro-L-tryptophan and of 5-fluoro-L-tryptophan catalyzed by tryptophan synthase: studies using fluorine-19 nuclear magnetic resonance and difference spectroscopy

Biochemistry ◽

10.1021/bi00363a011 ◽

1986 ◽

Vol 25 (15) ◽

pp. 4240-4249 ◽

Author(s):

Edith Wilson Miles ◽

Robert S. Phillips ◽

Herman J. C. Yeh ◽

Louis A. Cohen

Keyword(s):

Nuclear Magnetic Resonance ◽

Magnetic Resonance ◽

Tryptophan Synthase ◽

Difference Spectroscopy ◽

Nuclear Magnetic

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Polymer-protomer transition of acetyl-CoA carboxylase occurs in vivo and varies with nutritional conditions.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(19)70420-7 ◽

1980 ◽

Vol 255 (21) ◽

pp. 10033-10035

Author(s):

B.A. Ashcraft ◽

W.S. Fillers ◽

S.L. Augustine ◽

S.D. Clarke

Keyword(s):

Acetyl Coa Carboxylase ◽

Nutritional Conditions

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Thermal inactivation of tryptophan synthase. Stabilization by protein-protein interaction and protein-ligand interaction.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(17)32629-7 ◽

1994 ◽

Vol 269 (16) ◽

pp. 11703-11706

Author(s):

S.B. Ruvinov ◽

E.W. Miles

Keyword(s):

Protein Interaction ◽

Thermal Inactivation ◽

Tryptophan Synthase ◽

Ligand Interaction ◽

Protein Protein Interaction ◽

Protein Ligand Interaction

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Evidence that mutations in a loop region of the alpha-subunit inhibit the transition from an open to a closed conformation in the tryptophan synthase bienzyme complex.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(18)42377-0 ◽

1992 ◽

Vol 267 (18) ◽

pp. 13028-13038

Author(s):

P.S. Brzović ◽

Y Sawa ◽

C.C. Hyde ◽

E.W. Miles ◽

M.F. Dunn

Keyword(s):

Alpha Subunit ◽

Tryptophan Synthase ◽

Closed Conformation ◽

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Mechanism of mutual activation of the tryptophan synthase alpha and beta subunits. Analysis of the reaction specificity and substrate-induced inactivation of active site and tunnel mutants of the beta subunit.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(18)54673-1 ◽

1991 ◽

Vol 266 (32) ◽

pp. 21548-21557 ◽

Author(s):

S.A. Ahmed ◽

S.B. Ruvinov ◽

A.M. Kayastha ◽

E.W. Miles

Keyword(s):

Active Site ◽

Beta Subunit ◽

Beta Subunits ◽

Tryptophan Synthase ◽

Reaction Specificity

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Evidence for two conformers of the beta subunit of tryptophan synthase in solution

Journal of Biological Chemistry ◽

10.1016/s0021-9258(18)50092-2 ◽

1992 ◽

Vol 267 (32) ◽

pp. 23309-23317

Author(s):

S.A. Ahmed ◽

E.W. Miles

Keyword(s):

Beta Subunit ◽

Tryptophan Synthase

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