EC Number   |
General Information |
Reference |
|---|
   4.1.99.14 | malfunction |
contrary to the C140A mutant, the double mutant repaires the DNA lesion without generating DNA adducts. Furthermore, in the crystal structure, the mutant S76C is shown to be at 4.1 A from the methylene bridge of SP which is a shorter distance than the one reported for the wild-type enzyme |
-, 748852 |
| 4.1.99.14 | malfunction |
mutation at the remote glycine 168 residue alters the enzyme 3D structure, subsequently reducing the SPL activity by changing the positions of the essential amino acids involved in the radical transfer process |
-, 747837 |
| 4.1.99.14 | malfunction |
the enzyme C141A mutant produces thymidylyl-(3'->5')-thymidylate likely via an unprecedented thymine radical cation reduction (proton coupled electron transfer) mechanism |
-, 726998 |
| 4.1.99.14 | more |
a cysteine and two tyrosine residues are located in proximity and able to participate in the radical transfer process during the enzyme catalysis |
-, 747837 |
| 4.1.99.14 | more |
active site structure of Gt SPL in complex with substrate and S-adenosyl-L-methionine, Cys140, Tyr96, and Tyr98 are active site residues, overview |
-, 748201 |
| 4.1.99.14 | more |
active site structure, DNA lesion recognition, and substrate binding which involve a beta-hairpin structure, overview. S-adenosyl-L-methionine and a conserved cysteine residue are perfectly positioned in the active site for hydrogen atom abstraction from the dihydrothymine residue of the lesion and donation to the alpha-thyminyl radical moiety, respectively. Structure comparison of wild-type and C140 mutant enzymes, overview |
-, 728401 |
| 4.1.99.14 | more |
combined Mössbauer, multi-edge X-ray absorption spectroscopic, and density functional theoretical study of theradical SAM enzyme spore photoproduct lyase, detailed overview. SPL requires S-adenosyl-L-methionine (SAM) and a redox active [4Fe-4S] cluster for catalysis |
-, 748241 |
| 4.1.99.14 | more |
conformational changes associated with cofactor and substrate binding may serve to provide a solvent inaccessible and protected active site to safely catalyze radical reactions |
-, 747765 |
| 4.1.99.14 | more |
Cys141, Tyr97, and Tyr99 are active site residues |
-, 748201 |
| 4.1.99.14 | more |
residue C141 is solvent exposable and no other protein residue locates between the thymidylyl-(3'->5')-thymidylate radical and the C141 in the wild--type enzyme reaction pathway |
-, 726998 |
