EC Number   |
Protein Variants |
Reference |
|---|
   1.3.7.12 | F218V |
a mutant protein that produces the stereoisomer of primary fluorescent chlorophyll catabolites at the C1 position, the F218V mutation changes the stereospecificity in RCCR. Construction of wild-type and F218V mutant RCCR lacking the chloroplast transit peptide, Met1 to Gln39, i.e. RCCRDELTA49 |
712769 |
| 1.3.7.12 | F218V |
mutation switches At-RCCR stereospecificity from pFCC-1 to pFCC-2 production |
676436 |
| 1.3.7.12 | F218V |
the AtRCCR mutant protein produces the stereoisomer of primary fluorescent chlorophyll catabolites at the C1 position. The RCC in F218V AtRCCR rotates slightly compared with that in wild-type to fill in the space generated by the substitution of Phe218 with valine. Concomitantly, the two carboxy groups of Glu154 and Asp291 move slightly away from the C20/C1 double bond. Analysis of substrate-free and substrate-bound enzyme crystal structures, and comparison to wild-type structures, overview |
712769 |
| 1.3.7.12 | M729G |
a naturally occuring green pod mutant |
763069 |
| 1.3.7.12 | M729Y |
a naturally occuring yellow pod mutant |
763069 |
| 1.3.7.12 | more |
chimeric RCCRs are produced in Escherichia coli by replacing parts of mature enzyme from Arabidopsis thaliana with the respective sequences from Lycopersicon esculentum. A reversal of specificity is found in protein M, in which a domain of 37 amino acids of At-RCCR have been replaced with the respective Le-RCCR domain |
676436 |
| 1.3.7.12 | more |
chimeric RCCRs composed of portions of the Arabidopsis and the tomato proteins are expressed in Escherichia coli |
671354 |
| 1.3.7.12 | more |
construction of chimeric enzymes composed of portions of the Arabidopsis and the tomato proteins and expression in Escherichia coli, functional complementation of Arabidopsis acd2-2 mutant |
735438 |
| 1.3.7.12 | more |
construction of N-terminally truncated variants of wild-type enzyme and enzyme mutant F218V, i.e. AtRCCRDELTA49 and F218V AtRCCRDELTA49 |
712769 |
| 1.3.7.12 | more |
in the homologous system with both components from barley leaves, the slightly more polar pFCC-1 is produced, whereas the combination of barley membranes with soluble protein from spinach yields the less polar pFCC-2 |
676395 |
