Tags

Type your tag names separated by a space and hit enter

Structural basis for aconitase activity inactivation by butanedione and binding of substrates and inhibitors.
Biochim Biophys Acta. 1977 Oct 13; 484(2):453-64.BB

Abstract

Aconitase (citrate(isocitrate)hydro-lyase, EC 4.2.1.3) prior to activation demonstrates a single binding site for substrates and inhibitors. On the basis of kinetic experiments, at pH 8.5 and 37 degrees C, with monomeric butanedione in borate, this binding site was found to contain a single arginine residue. Dissociation constants at pH 8.5 and 37 degrees C, determined from inhibitory effects on butanedione inactivation rates are: citrate, 0.74 mM; D-isocitrate, 0.33 mM: cis-aconitate, 0.52 mM; tricarballytate, 0.42 mM; trans-aconitate, 0.025 mM. Corresponding dissociation constants for the active enzyme are: tricarballylate, 0.39 mM; trans-aconitate, 0.14 mM. Active site Fe2+ added to the enzyme on activation is therefore not required for binding. Km values are: citrate, 0.23 mM and cis-aconitate 0.012 mM. Binding to active enzyme is considered to be transition state binding.

Links

Publisher Full Text

Authors

Gawron O
No affiliation info available
Jones L
No affiliation info available

MeSH

Aconitate HydrataseAconitic AcidAnimalsArginineBinding SitesBinding, CompetitiveBoratesButanonesCitratesDiacetylIronKineticsSwine

Pub Type(s)

Journal Article
Research Support, U.S. Gov't, Non-P.H.S.
Research Support, U.S. Gov't, P.H.S.

Language

eng

PubMed ID

597359

Citation

Gawron, O, and L Jones. "Structural Basis for Aconitase Activity Inactivation By Butanedione and Binding of Substrates and Inhibitors." Biochimica Et Biophysica Acta, vol. 484, no. 2, 1977, pp. 453-64.
Gawron O, Jones L. Structural basis for aconitase activity inactivation by butanedione and binding of substrates and inhibitors. Biochim Biophys Acta. 1977;484(2):453-64.
Gawron, O., & Jones, L. (1977). Structural basis for aconitase activity inactivation by butanedione and binding of substrates and inhibitors. Biochimica Et Biophysica Acta, 484(2), 453-64.
Gawron O, Jones L. Structural Basis for Aconitase Activity Inactivation By Butanedione and Binding of Substrates and Inhibitors. Biochim Biophys Acta. 1977 Oct 13;484(2):453-64. PubMed PMID: 597359.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Structural basis for aconitase activity inactivation by butanedione and binding of substrates and inhibitors. AU - Gawron,O, AU - Jones,L, PY - 1977/10/13/pubmed PY - 1977/10/13/medline PY - 1977/10/13/entrez SP - 453 EP - 64 JF - Biochimica et biophysica acta JO - Biochim Biophys Acta VL - 484 IS - 2 N2 - Aconitase (citrate(isocitrate)hydro-lyase, EC 4.2.1.3) prior to activation demonstrates a single binding site for substrates and inhibitors. On the basis of kinetic experiments, at pH 8.5 and 37 degrees C, with monomeric butanedione in borate, this binding site was found to contain a single arginine residue. Dissociation constants at pH 8.5 and 37 degrees C, determined from inhibitory effects on butanedione inactivation rates are: citrate, 0.74 mM; D-isocitrate, 0.33 mM: cis-aconitate, 0.52 mM; tricarballytate, 0.42 mM; trans-aconitate, 0.025 mM. Corresponding dissociation constants for the active enzyme are: tricarballylate, 0.39 mM; trans-aconitate, 0.14 mM. Active site Fe2+ added to the enzyme on activation is therefore not required for binding. Km values are: citrate, 0.23 mM and cis-aconitate 0.012 mM. Binding to active enzyme is considered to be transition state binding. SN - 0006-3002 UR - https://www.unboundmedicine.com/medline/citation/597359/Structural_basis_for_aconitase_activity_inactivation_by_butanedione_and_binding_of_substrates_and_inhibitors_ L2 - https://linkinghub.elsevier.com/retrieve/pii/0005-2744(77)90101-2 DB - PRIME DP - Unbound Medicine ER -