Tags

Type your tag names separated by a space and hit enter

Study of anthranilate synthase function by replacement of cysteine 84 using site-directed mutagenesis.
J Biol Chem. 1985 Feb 10; 260(3):1889-94.JB

Abstract

Cysteine 84 was replaced by glycine in Serratia marcescens anthranilate synthase Component II using site-directed mutagenesis of cloned trpG. This replacement abolished the glutamine-dependent anthranilate synthase activity but not the NH3-dependent activity of the enzyme. The mutation provides further evidence for the role of active site cysteine 84 in the glutamine amide transfer function of anthranilate synthase Component II. By the criteria of circular dichroism, proteolytic inactivation, and feedback inhibition the mutant and wild type enzymes were structurally similar. The NH3-dependent anthranilate synthase activity of the mutant enzyme supported tryptophan synthesis in media containing a high concentration of ammonium ion.

Authors

Paluh JL
No affiliation info available
Zalkin H
No affiliation info available
Betsch D
No affiliation info available
Weith HL
No affiliation info available

MeSH

Amino Acid SequenceAmmoniaAnthranilate SynthaseBase SequenceCloning, MolecularCysteineDNA, BacterialEscherichia coliGlutamineMutationNucleic Acid HeteroduplexesPlasmidsProtein ConformationSerratia marcescensStructure-Activity Relationship

Pub Type(s)

Comparative Study
Journal Article
Research Support, U.S. Gov't, P.H.S.

Language

eng

PubMed ID

3881444

Citation

Paluh, J L., et al. "Study of Anthranilate Synthase Function By Replacement of Cysteine 84 Using Site-directed Mutagenesis." The Journal of Biological Chemistry, vol. 260, no. 3, 1985, pp. 1889-94.
Paluh JL, Zalkin H, Betsch D, et al. Study of anthranilate synthase function by replacement of cysteine 84 using site-directed mutagenesis. J Biol Chem. 1985;260(3):1889-94.
Paluh, J. L., Zalkin, H., Betsch, D., & Weith, H. L. (1985). Study of anthranilate synthase function by replacement of cysteine 84 using site-directed mutagenesis. The Journal of Biological Chemistry, 260(3), 1889-94.
Paluh JL, et al. Study of Anthranilate Synthase Function By Replacement of Cysteine 84 Using Site-directed Mutagenesis. J Biol Chem. 1985 Feb 10;260(3):1889-94. PubMed PMID: 3881444.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Study of anthranilate synthase function by replacement of cysteine 84 using site-directed mutagenesis. AU - Paluh,J L, AU - Zalkin,H, AU - Betsch,D, AU - Weith,H L, PY - 1985/2/10/pubmed PY - 1985/2/10/medline PY - 1985/2/10/entrez SP - 1889 EP - 94 JF - The Journal of biological chemistry JO - J Biol Chem VL - 260 IS - 3 N2 - Cysteine 84 was replaced by glycine in Serratia marcescens anthranilate synthase Component II using site-directed mutagenesis of cloned trpG. This replacement abolished the glutamine-dependent anthranilate synthase activity but not the NH3-dependent activity of the enzyme. The mutation provides further evidence for the role of active site cysteine 84 in the glutamine amide transfer function of anthranilate synthase Component II. By the criteria of circular dichroism, proteolytic inactivation, and feedback inhibition the mutant and wild type enzymes were structurally similar. The NH3-dependent anthranilate synthase activity of the mutant enzyme supported tryptophan synthesis in media containing a high concentration of ammonium ion. SN - 0021-9258 UR - https://www.unboundmedicine.com/medline/citation/3881444/Study_of_anthranilate_synthase_function_by_replacement_of_cysteine_84_using_site_directed_mutagenesis_ DB - PRIME DP - Unbound Medicine ER -
Grapherence [↓14]

Related Citations

More