EC Number   |
Posttranslational Modification |
Reference |
|---|
    1.13.11.20 | more |
a unique post-translational modification of human CDO consisting of a cross-link between cysteine 93 and tyrosine 157 (Cys-Tyr), which increases catalytic efficiency in a substrate-dependent manner |
741585 |
| 1.13.11.20 | more |
Cys93-Sgamma is covalently bound to Tyr157-Cepsilon2 forming a cysteinyl-tyronsine linkage. |
674591 |
| 1.13.11.20 | more |
residues C93-Y157 crosslink as a result of a posttranslational modification |
742264 |
| 1.13.11.20 | more |
the enzyme activity is in part modulated by the formation of a Cys93-Tyr157 crosslink that increases its catalytic efficiency over 10fold, mechanism, overview. The crosslink enhances activity by positioning the Tyr157 hydroxyl to enable proper Cys binding, proper oxygen binding, and optimal chemistry |
743088 |
| 1.13.11.20 | more |
the residues Tyr-157 and Cys-93 appear to be covalently linked between Tyr-157 CE and Cys-93 SG, because these two atoms lie within 2.2 A |
676850 |
| 1.13.11.20 | more |
two posttranslational modifications adjacent to the catalytic iron center: a thioether cross-link between Cys93 and Tyr157 and extra electron density at Cys164 which is variously explained as cystine or cysteine sulfinic acid |
699024 |
| 1.13.11.20 | no modification |
no posttranslational modification observed |
-, 759471 |
