Literature summary 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 .
Protein Variants
EC Number |
Protein Variants |
Comment |
Organism |
---|
1.1.3.17 |
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 |
1.1.3.17 |
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 |
1.1.3.17 |
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
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
1.1.3.17 |
Arthrobacter globiformis |
Q7X2H8 |
- |
- |
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
1.1.3.17 |
codA |
- |
Arthrobacter globiformis |
General Information
EC Number |
General Information |
Comment |
Organism |
---|
1.1.3.17 |
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 |