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Literature summary for 4.1.99.14 extracted from
- Spore photoproduct lyase the known, the controversial, and the unknown (2015), J. Biol. Chem., 290, 4003-4009 .
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| C141A | site-directed mutagenesis, spores carrying the C141A mutation are sensitive to UV irradiation | Bacillus subtilis |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Fe2+ | [4Fe-4S] cluster, SPL is an iron-sulfur enzyme | Geobacillus thermodenitrificans |  |
| Fe2+ | [4Fe-4S] cluster, SPL is an iron-sulfur enzyme | Bacillus subtilis | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| (5R)-5,6-dihydro-5-(thymidin-7-yl)thymidine | Geobacillus thermodenitrificans | in double-helical DNA | thymidylyl-(3'->5')-thymidylate | - |
? | |
| (5R)-5,6-dihydro-5-(thymidin-7-yl)thymidine | Bacillus subtilis | in double-helical DNA | thymidylyl-(3'->5')-thymidylate | - |
? | |
| (5R)-5,6-dihydro-5-(thymidin-7-yl)thymidine | Bacillus subtilis 168 | in double-helical DNA | thymidylyl-(3'->5')-thymidylate | - |
? | |
| (5R)-5,6-dihydro-5-(thymidin-7-yl)thymidine | Geobacillus thermodenitrificans NG80-2 | in double-helical DNA | thymidylyl-(3'->5')-thymidylate | - |
? | |
| additional information | Geobacillus thermodenitrificans | DNA conformation during in vivo repair and dinucleotide SP TpT flipping process, overview | ? | - |
? | |
| additional information | Bacillus subtilis | DNA conformation during in vivo repair and dinucleotide SP TpT flipping process, overview | ? | - |
? | |
| additional information | Bacillus subtilis 168 | DNA conformation during in vivo repair and dinucleotide SP TpT flipping process, overview | ? | - |
? | |
| additional information | Geobacillus thermodenitrificans NG80-2 | DNA conformation during in vivo repair and dinucleotide SP TpT flipping process, overview | ? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bacillus subtilis | P37956 | - |
- |
| Bacillus subtilis 168 | P37956 | - |
- |
| Geobacillus thermodenitrificans | A4IQU1 | - |
- |
| Geobacillus thermodenitrificans NG80-2 | A4IQU1 | - |
- |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| (5R)-5,6-dihydro-5-(thymidin-7-yl)thymidine (in double-helical DNA) = thymidylyl-(3'->5')-thymidylate (in double-helical DNA) | SPL is a radical S-adenosylmethionine (SAM) enzyme, reaction mechanism, detailed overview. Radicals are quenched to close the catalytic cycle. The characteristic CXXXCXXC motif is involved in catalysis, although other tri-cysteine motifs may also facilitate this radical chemistry. Enzyme SPL directly directly reverts SP thymine photodimer. The conserved solvent-accessible cysteine 140 is the intrinsic hydrogen atom donor | Geobacillus thermodenitrificans | |
| (5R)-5,6-dihydro-5-(thymidin-7-yl)thymidine (in double-helical DNA) = thymidylyl-(3'->5')-thymidylate (in double-helical DNA) | SPL is a radical S-adenosylmethionine (SAM) enzyme, reaction mechanism, detailed overview. Radicals are quenched to close the catalytic cycle. The characteristic CXXXCXXC motif is involved in catalysis, although other tri-cysteine motifs may also facilitate this radical chemistry. Enzyme SPL directly reverts SP thymine photodimer. The conserved solvent-accessible cysteine 141 is the intrinsic hydrogen atom donor to the thymine radical | Bacillus subtilis |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| (5R)-5,6-dihydro-5-(thymidin-7-yl)thymidine | in double-helical DNA | Geobacillus thermodenitrificans | thymidylyl-(3'->5')-thymidylate | - |
? | |
| (5R)-5,6-dihydro-5-(thymidin-7-yl)thymidine | in double-helical DNA | Bacillus subtilis | thymidylyl-(3'->5')-thymidylate | - |
? | |
| (5R)-5,6-dihydro-5-(thymidin-7-yl)thymidine | in double-helical DNA | Bacillus subtilis 168 | thymidylyl-(3'->5')-thymidylate | - |
? | |
| (5R)-5,6-dihydro-5-(thymidin-7-yl)thymidine | in double-helical DNA | Geobacillus thermodenitrificans NG80-2 | thymidylyl-(3'->5')-thymidylate | - |
? | |
| additional information | DNA conformation during in vivo repair and dinucleotide SP TpT flipping process, overview | Geobacillus thermodenitrificans | ? | - |
? | |
| additional information | DNA conformation during in vivo repair and dinucleotide SP TpT flipping process, overview | Bacillus subtilis | ? | - |
? | |
| additional information | DNA conformation during in vivo repair and dinucleotide SP TpT flipping process, overview | Bacillus subtilis 168 | ? | - |
? | |
| additional information | DNA conformation during in vivo repair and dinucleotide SP TpT flipping process, overview | Geobacillus thermodenitrificans NG80-2 | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| Bs SPL | - |
Bacillus subtilis |
| Gt SPL | - |
Geobacillus thermodenitrificans |
| SPL | - |
Geobacillus thermodenitrificans |
| SPL | - |
Bacillus subtilis |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| S-adenosyl-L-methionine | SPL is a radical SAM enzyme | Geobacillus thermodenitrificans | |
| S-adenosyl-L-methionine | SPL is a radical SAM enzyme | Bacillus subtilis | |
| [4Fe-4S] cluster | SPL is an iron-sulfur enzyme | Geobacillus thermodenitrificans | |
| [4Fe-4S] cluster | SPL is an iron-sulfur enzyme | Bacillus subtilis | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | the enzyme is a member of the radical SAM superfamily, which is defined by the characteristic CXXXCXXC motif | Geobacillus thermodenitrificans |
| evolution | the enzyme is a member of the radical SAM superfamily, which is defined by the characteristic CXXXCXXC motif | Bacillus subtilis |
| additional information | active site structure of Gt SPL in complex with substrate and S-adenosyl-L-methionine, Cys140, Tyr96, and Tyr98 are active site residues, overview | Geobacillus thermodenitrificans |
| additional information | Cys141, Tyr97, and Tyr99 are active site residues | Bacillus subtilis |
| physiological function | spore photoproduct lyase (SPL) repairs 5-thyminyl-5,6-dihydrothymine, a thymine dimer that is also called the spore photoproduct (SP), in germinating endospores. SPL is a radical S-adenosylmethionine (SAM) enzyme, utilizing the 5'-deoxyadenosyl radical generated by SAM reductive cleavage reaction to revert SP to two thymine residues | Geobacillus thermodenitrificans |
| physiological function | spore photoproduct lyase (SPL) repairs 5-thyminyl-5,6-dihydrothymine, a thymine dimer that is also called the spore photoproduct (SP), in germinating endospores. SPL is a radical S-adenosylmethionine (SAM) enzyme, utilizing the 5'-deoxyadenosyl radical generated by SAM reductive cleavage reaction to revert SP to two thymine residues | Bacillus subtilis |
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