Any feedback?
Please rate this page
(search_result.php)
(0/150)

BRENDA support

Refine search

Search Metals/Ions

show results
Don't show organism specific information (fast!)
Search organism in taxonomic tree (slow, choose "exact" as search mode, e.g. "mammalia" for rat,human,monkey,...)
(Not possible to combine with the first option)
Refine your search
Image of 2D Structure

Search term:

Results 1 - 10 of 13 > >>
EC Number Metals/Ions Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 1.1.99.35Ca2+ 0.5 mM used in assay conditions 739914
Display the word mapDisplay the reaction diagram Show all sequences 1.1.99.35Ca2+ calcium is essential for dimerization and PQQ binding 762778
Display the word mapDisplay the reaction diagram Show all sequences 1.1.99.35Ca2+ or Cd2+, Sr2+, or Mn2+, required for binding of cofactor PQQ in soluble isoform sGDH, 100% activity with Ca2+. Mg2+, or Ca2+, Zn2+, or Sr2+, required for binding of cofactor PQQ in membrane-bound isoform mGDH. 100% activity with Ca2+ 702726
Display the word mapDisplay the reaction diagram Show all sequences 1.1.99.35Ca2+ reconstitution mechanism of the enzyme (sGDH) with its two cofactors, i.e., pyrroloquinoline quinone (PQQ) and Ca2+: pyrroloquinoline quinone first binds to apo-sGDH, it strongly impedes the access of Ca2+ to its enclosed position at the bottom of the enzyme binding site, thereby greatly slowing down the reconstitution rate of sGDH. The slow calcium insertion may purposely be accelerated by providing more flexibility to the Ca2+ binding loop through the specific mutation of the calcium-coordinating P248 proline residue, reducing thus the kinetic barrier to calcium ion insertion 762554
Display the word mapDisplay the reaction diagram Show all sequences 1.1.99.35Ca2+ study on interconversions of different enzyme species from monomeric apoenzyme to fully reconstituted enzyme, e.g. consisting of dimer with one firmly bound Ca2+ ion, dimer with two PQQ and two extra Ca2+ ions, or substitutes for Ca2+. Dimers consisting of two monomers with one firmly bound Ca2+ ion and dimers consisting of two monomers with one firmly bound Ca2+ ion and with two PQQ and two extra Ca2+ ions are very stable enzyme species regarding monomerization and inactivation by chelator, respectively, the bound Ca2+ being locked up in such a way that it is not accessible to chelator. The two Ca2+ ions required for activation of dimers consisting of two monomers with one firmly bound Ca2+ ion and with two PQQ, are even more firmly bound than the two required for dimerization of monomers and anchoring of PQQ 703530
Display the word mapDisplay the reaction diagram Show all sequences 1.1.99.35Ca2+ substituting the Ca2+ involved in activation of pyrroloquinoline quinone in soluble GDH by Sr2+ affects the cooperativity effect but not the two turnover rates of the hybrid enzyme for glucose 703532
Display the word mapDisplay the reaction diagram Show all sequences 1.1.99.35Ca2+ the enzyme binds three calcium ions per monomer, two of which are located in the dimer interface, crystallization data 639204
Display the word mapDisplay the reaction diagram Show all sequences 1.1.99.35Ca2+ the holoenzyme is reconstituted by incubating the apoenzyme in 5 mM MES buffer at pH 6.5 with 1 mM CaCl2 and 0.060 mM pyrroloquinoline quinone for 3 h at room temperature in the dark 762834
Display the word mapDisplay the reaction diagram Show all sequences 1.1.99.35Cd2+ or Ca2+, Sr2+, or Mn2+, required for binding of cofactor PQQ in soluble isoform sGDH. Mg2+, or Ca2+, Zn2+, or Sr2+, required for binding of cofactor PQQ in membrane-bound isoform mGDH 702726
Display the word mapDisplay the reaction diagram Show all sequences 1.1.99.35Mg2+ or Ca2+, Zn2+, or Sr2+, required for binding of cofactor PQQ in membrane-bound isoform mGDH. With Mg2+, 115% of the activity with Ca2+ 702726
Results 1 - 10 of 13 > >>