Literature summary for 1.1.3.17 extracted from

Su, D.; Yuan, H.; Gadda, G.
A reversible, charge-induced intramolecular C4a-S-cysteinyl-flavin in choline oxidase variant S101C (2017), Biochemistry, 56, 6677-6690 .

Search for more literature for 1.1.3.17

Protein Variants

Protein Variants	Comment	Organism
S101A	similar to wild-type mutant displays in 20 mM Tris-HCl flavin maxima in the near-UV and visible regions typical of oxidized flavins	Arthrobacter globiformis
S101C	in presence of protonated Tris in the active site, the reversible formation of a C4a-S-cysteinyl8alpha-N3-histidyl flavin is observed	Arthrobacter globiformis
S101T	similar to wild-type mutant displays in 20 mM Tris-HCl flavin maxima in the near-UV and visible regions typical of oxidized flavins	Arthrobacter globiformis

Organism

Organism	UniProt	Comment	Textmining
Arthrobacter globiformis	Q7X2H8	-	-

Synonyms

Synonyms	Comment	Organism
codA	-	Arthrobacter globiformis

General Information

General Information	Comment	Organism
metabolism	in mutant S101C, formation of the C4a-S-cysteinylflavin linkage between the side chain of C101 and the 8alpha-N3-histidyl flavin in the active site is triggered by the binding of protonated Tris in the active site of the enzyme. The C4a-S-cysteinyl-flavin is stabilized between about pH 7.0 and pH 9.5, in which the side chain of C101 is unprotonated and the N5 atom of the C4a-S-cysteinyl-flavin is protonated. The presence of Tris bound at the active site of the enzyme is required to deprotonate the cysteine and to trigger the formation of the C4a-S-cysteinyl-flavin, and for the stabilization of the C4a-S-cysteinyl-flavin	Arthrobacter globiformis

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Release 2023.1 (January 2023)