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Literature summary for 4.1.99.17 extracted from

  • Zhang, Q.; Liu, W.
    Complex biotransformations catalyzed by radical S-adenosylmethionine enzymes (2011), J. Biol. Chem., 286, 30245-30252.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 4.1.99.17

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ the enzyme contains a [4Fe-4S] cluster bound by the CXXCXXXXC motif Caulobacter vibrioides
Fe2+ the enzyme contains a [4Fe-4S] cluster bound by the CXXCXXXXC motif Salmonella enterica

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
5-amino-1-(5-phospho-D-ribosyl)imidazole + S-adenosyl-L-methionine Caulobacter vibrioides
-
 4-amino-2-methyl-5-phosphomethylpyrimidine + 5'-deoxyadenosine + L-methionine + formate + CO
-
 ?
5-amino-1-(5-phospho-D-ribosyl)imidazole + S-adenosyl-L-methionine Salmonella enterica
-
 4-amino-2-methyl-5-phosphomethylpyrimidine + 5'-deoxyadenosine + L-methionine + formate + CO
-
 ?

Organism

Organism UniProt Comment Textmining
Caulobacter vibrioides Q9A6Q5 gene thiC
-
Salmonella enterica Q9L9I7 subsp. enterica, serovar Typhimurium LT2, gene thiC
-

Reaction

Reaction Comment Organism Reaction ID
5-amino-1-(5-phospho-D-ribosyl)imidazole + S-adenosyl-L-methionine = 4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine + 5'-deoxyadenosine + L-methionine + formate + CO radical reaction mechanism, overview Caulobacter vibrioides
a
5-amino-1-(5-phospho-D-ribosyl)imidazole + S-adenosyl-L-methionine = 4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine + 5'-deoxyadenosine + L-methionine + formate + CO radical reaction mechanism, overview Salmonella enterica
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5-amino-1-(5-phospho-D-ribosyl)imidazole + S-adenosyl-L-methionine
-
 Caulobacter vibrioides 4-amino-2-methyl-5-phosphomethylpyrimidine + 5'-deoxyadenosine + L-methionine + formate + CO
-
 ?
5-amino-1-(5-phospho-D-ribosyl)imidazole + S-adenosyl-L-methionine
-
 Salmonella enterica 4-amino-2-methyl-5-phosphomethylpyrimidine + 5'-deoxyadenosine + L-methionine + formate + CO
-
 ?
5-amino-1-(5-phospho-D-ribosyl)imidazole + S-adenosyl-L-methionine optimal assay condition is set both by using flavodoxin, flavodoxin reductase, and NADPH to reduce the [4Fe-4S] cluster of ThiC and by obviation of the prolonged reaction time to minimize the uncoupled AdoH production Caulobacter vibrioides 4-amino-2-methyl-5-phosphomethylpyrimidine + 5'-deoxyadenosine + L-methionine + formate + CO
-
 ?
5-amino-1-(5-phospho-D-ribosyl)imidazole + S-adenosyl-L-methionine optimal assay condition is set both by using flavodoxin, flavodoxin reductase, and NADPH to reduce the [4Fe-4S] cluster of ThiC and by obviation of the prolonged reaction time to minimize the uncoupled AdoH production Salmonella enterica 4-amino-2-methyl-5-phosphomethylpyrimidine + 5'-deoxyadenosine + L-methionine + formate + CO
-
 ?

Synonyms

Synonyms Comment Organism
HMP-P synthase
-
 Caulobacter vibrioides
HMP-P synthase
-
 Salmonella enterica
thiC
-
 Caulobacter vibrioides
thiC
-
 Salmonella enterica

Cofactor

Cofactor Comment Organism Structure
S-adenosyl-L-methionine a S-adenosyl-L-methionine radical enzyme Caulobacter vibrioides
S-adenosyl-L-methionine a S-adenosyl-L-methionine radical enzyme Salmonella enterica

General Information

General Information Comment Organism
evolution the enzyme is a member of the radical S-adenosylmethionine (AdoMet) superfamily, reactions catalyzed by the radical AdoMet superfamily include mainly glycyl radical generation, sulfur insertion, methylation, methylthiolation, oxidation, isomerization, elimination (fragmentation), overview. ThiC does not contain the canonical CXXXCXXC motif in the N-terminal domain, as do most of the radical AdoMet enzymes, but a CXXCXXXXC motif Caulobacter vibrioides
evolution the enzyme is a member of the radical S-adenosylmethionine (AdoMet) superfamily, reactions catalyzed by the radical AdoMet superfamily include mainly glycyl radical generation, sulfur insertion, methylation, methylthiolation, oxidation, isomerization, elimination (fragmentation), overview. ThiC does not contain the canonical CXXXCXXC motif in the N-terminal domain, as do most of the radical AdoMet enzymes, but a CXXCXXXXC motif Salmonella enterica
metabolism the enzyme is important in thiamine biosynthesis, an essential compound in all living organisms that participates in several key cellular processes, such as carbohydrate and amino acid metabolism. Thiamine consists of a thiazole and a pyrimidine heterocycle, which are synthesized separately and assembled together by thiamine phosphate synthase Caulobacter vibrioides
metabolism the enzyme is important in thiamine biosynthesis, an essential compound in all living organisms that participates in several key cellular processes, such as carbohydrate and amino acid metabolism. Thiamine consists of a thiazole and a pyrimidine heterocycle, which are synthesized separately and assembled together by thiamine phosphate synthase Salmonella enterica