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Literature summary for 4.1.99.14 extracted from

  • Silver, S.C.; Gardenghi, D.J.; Naik, S.G.; Shepard, E.M.; Huynh, B.H.; Szilagyi, R.K.; Broderick, J.B.
    Combined Moessbauer spectroscopic, multi-edge X-ray absorption spectroscopic, and density functional theoretical study of the radical SAM enzyme spore photoproduct lyase (2014), J. Biol. Inorg. Chem., 19, 465-483 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 4.1.99.14

Cloned(Commentary)

Cloned (Comment) Organism
gene splB, recombinant expression of N-terminal His6-tagged enzyme in Escherichia coli strain Tuner(DE3)pLysS Clostridium acetobutylicum

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 Clostridium acetobutylicum in double-helical DNA thymidylyl-(3'->5')-thymidylate
-
 ?
(5R)-5,6-dihydro-5-(thymidin-7-yl)thymidine Clostridium acetobutylicum ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787 in double-helical DNA thymidylyl-(3'->5')-thymidylate
-
 ?

Organism

Organism UniProt Comment Textmining
Clostridium acetobutylicum Q97L63
-
-
Clostridium acetobutylicum ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787 Q97L63
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-

Purification (Commentary)

Purification (Comment) Organism
recombinant N-terminal His6-tagged enzyme from Escherichia coli strain Tuner(DE3)pLysS by nickel affinity chromatography, anaerobic dialysis, and ultrafiltration Clostridium acetobutylicum

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) SP repair is initiated by abstraction of a H atom from C6 of SP. The SP(C6) substrate radical is thought to promote a radical-mediated beta-scission of the C-C bond linking the two thymines; the resulting product radical then abstracts an H atom to generate repaired thymine. S-adenosyl-L-methionine as a substrate utilize a defined dinucleotide or dinucleoside SP, rather than SP in intact DNA, suggesting the possibility that stoichiometric SAM cleavage is favored with non-optimal substrates Clostridium acetobutylicum
a

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 Clostridium acetobutylicum thymidylyl-(3'->5')-thymidylate
-
 ?
(5R)-5,6-dihydro-5-(thymidin-7-yl)thymidine in double-helical DNA Clostridium acetobutylicum ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787 thymidylyl-(3'->5')-thymidylate
-
 ?

Synonyms

Synonyms Comment Organism
SplB
-
 Clostridium acetobutylicum

Cofactor

Cofactor Comment Organism Structure
S-adenosyl-L-methionine SAM, SPL is a radical SAM enzyme and requires S-adenosyl-L-methionine (SAM) for catalysis. Density functional theory calculations provide insights into structural and electronic perturbations that can be correlated by considering the role of SAM as a catalyst or substrate. Mapping of the [4Fe-4S]/SAM interaction, and speciation dependent SAM/cluster interactions Clostridium acetobutylicum
[4Fe-4S] cluster enzyme SPL requires a redox active [4Fe-4S] cluster for catalysis. Mossbauer analysis of anaerobically purified SPL indicates the presence of a mixture of cluster states with the majority (40%) as [2Fe-2S]2+ and a smaller amount (15%) as [4Fe-4S]2+ clusters. Upon reduction, the cluster content changes to primarily (60%) [4Fe-4S]+. Mapping of the [4Fe-4S]/SAM interaction, and speciation dependent SAM/cluster interactions Clostridium acetobutylicum

General Information

General Information Comment Organism
evolution spore photoproduct lyase (SPL) is a member of the radical S-adenosyl-L-methionine (SAM) superfamily, the family members utilize S-adenosyl-Lmethionine (SAM) and a redox active [4Fe-4S] cluster to carry out diverse radical reactions including rearrangements, sulfur insertions and oxidations. Electron-nuclear double resonance and X-ray crystallography of several members of the superfamily have shown that the unique iron is coordinated by the amino and carboxylate moieties of S-adenosyl-L-methionine. An innersphere electron transfer from a reduced [4Fe-4S]+ cluster to the sulfonium of SAM leads to homolytic S-C(5') bond cleavage to generate a 5'-deoxyadenosyl radical (dAdo) intermediate, which abstracts a hydrogen atom from substrate to initiate a radical transformation Clostridium acetobutylicum
additional information 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 Clostridium acetobutylicum
physiological function spore photoproduct lyase (SPL) catalyzes the direct reversal of a specific DNA photoproduct, 5-thyminyl-5,6-dihydrothymine (spore photoproduct or SP), back to two thymines. The methylene-bridged thymine dimer SP is the primary photoproduct when bacterial spores are subjected to UV radiation, and is rapidly repaired upon spore germination Clostridium acetobutylicum