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Literature summary for 4.1.99.14 extracted from

  • Chandor, A.; Berteau, O.; Douki, T.; Gasparutto, D.; Sanakis, Y.; Ollagnier-de-Choudens, S.; Atta, M.; Fontecave, M.
    Dinucleotide spore photoproduct, a minimal substrate of the DNA repair spore photoproduct lyase enzyme from Bacillus subtilis (2006), J. Biol. Chem., 281, 26922-26931.
    View publication on PubMed
Search for more literature for 4.1.99.14

Activating Compound

Activating Compound Comment Organism Structure
DTT
-
 Bacillus subtilis

Cloned(Commentary)

Cloned (Comment) Organism
gene splB, overexpression of N-terminally His-tagged enzyme in Escherichia coli strain Tuner (DE3) Bacillus subtilis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information kinetics Bacillus subtilis

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ the enzyme is an S-adenosylmethionine-dependent [4Fe-4S]2+ protein, spectral analysis, overview 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 (in double helical DNA) + S-adenosyl-L-methionine + 2 H+ Bacillus subtilis
-
 thymidylyl-(3'-5')-thymidylate (in DNA) + 5'-deoxyadenosine + L-methionine
-
 ?
additional information Bacillus subtilis the (5R)-5,6-dihydro-5-(thymidin-7-yl)thymidine lesion does not absolutely need to be contained within a single or double-stranded DNA for recognition and repaired by the enzyme ?
-
 ?

Organism

Organism UniProt Comment Textmining
Bacillus subtilis
-
 gene splB
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzyme from Escherichia coli strain Tuner (DE3) by nickel affinity chromatography Bacillus subtilis

Source Tissue

Source Tissue Comment Organism Textmining

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) + S-adenosyl-L-methionine + 2 H+
-
 Bacillus subtilis thymidylyl-(3'-5')-thymidylate (in DNA) + 5'-deoxyadenosine + L-methionine
-
 ?
additional information the (5R)-5,6-dihydro-5-(thymidin-7-yl)thymidine lesion does not absolutely need to be contained within a single or double-stranded DNA for recognition and repaired by the enzyme Bacillus subtilis ?
-
 ?

Synonyms

Synonyms Comment Organism
More the SP lyase is an S-adenosyl-L-methionine-dependent iron-sulfur protein that belongs to the radical S-adenosylmethionine superfamily Bacillus subtilis
SP lyase
-
 Bacillus subtilis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Bacillus subtilis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
 assay at Bacillus subtilis

Cofactor

Cofactor Comment Organism Structure
S-adenosyl-L-methionine the enzyme is an S-adenosylmethionine-dependent iron-sulfur protein that belongs to the radical S-adenosylmethionine superfamily Bacillus subtilis

General Information

General Information Comment Organism
physiological function the overwhelming majority of DNA photoproducts in UV-irradiated spores is a unique thymine dimer called spore photoproduct, SP, or 5-thymine-5,6-dihydrothymine. This lesion is repaired by the spore photoproduct lyase enzyme that directly reverts 5-thymine-5,6-dihydrothymine to two unmodified thymines. The SP lyase enzyme demonstrates an aspect of the diversity of DNA repair mechanisms in living organisms Bacillus subtilis