v5.1.0.3
Cicer data from the Legume Information System
Description | The formation of the fluorescent protein FP611 chromophore cross-link from the alpha-carboxyl carbon of residue n, a methionine, to the alpha-amino nitrogen of residue n+2, a glycine, and a dehydration to form a double bond to the alpha-amino nitrogen of residue n+1. This cross-linking is coupled with a dehydrogenation of residue n+1 to form a double bond between the alpha and beta carbons. This modification is found in the GFP-like fluorescent chromoprotein from the sea anemone Entacmaea quadricolor. |
Namespace | biological_process |
Obsolete | false |