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Literature summary for 2.1.2.B2 extracted from

  • Chen, C.; Gao, T.; Zhao, G.; Deng, Z.; Hu, S.; Xu, H.; He, X.
    Evidence from 18O feeding studies for hydroxyl group donor in the reaction catalyzed by cytidylate hydroxymethylase MilA (2013), Chin. Sci. Bull., 58, 864-868.
No PubMed abstract available

Cloned(Commentary)

Cloned (Comment) Organism
gene milA, sequence comparisons, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) Streptomyces rimofaciens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
5,10-methylenetetrahydrofolate + H2O + cytidylate Streptomyces rimofaciens
-
tetrahydrofolate + 5-hydroxymethylcytidylate
-
?
5,10-methylenetetrahydrofolate + H2O + cytidylate Streptomyces rimofaciens ZJU5119
-
tetrahydrofolate + 5-hydroxymethylcytidylate
-
?
additional information Streptomyces rimofaciens 5-hydroxymethylcytosine is present in a nucleoside antibiotic mildiomycin and its formation is governed by a cytidylate hydroxymethylase MilA ?
-
?
additional information Streptomyces rimofaciens ZJU5119 5-hydroxymethylcytosine is present in a nucleoside antibiotic mildiomycin and its formation is governed by a cytidylate hydroxymethylase MilA ?
-
?

Organism

Organism UniProt Comment Textmining
Streptomyces rimofaciens
-
gene milA
-
Streptomyces rimofaciens ZJU5119
-
gene milA
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography Streptomyces rimofaciens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5,10-methylenetetrahydrofolate + H2O + cytidylate
-
Streptomyces rimofaciens tetrahydrofolate + 5-hydroxymethylcytidylate
-
?
5,10-methylenetetrahydrofolate + H2O + cytidylate
-
Streptomyces rimofaciens ZJU5119 tetrahydrofolate + 5-hydroxymethylcytidylate
-
?
additional information 5-hydroxymethylcytosine is present in a nucleoside antibiotic mildiomycin and its formation is governed by a cytidylate hydroxymethylase MilA Streptomyces rimofaciens ?
-
?
additional information MilA uses solvent water as the hydroxyl group donor like cytidylate hydroxymethylase. Thr102 of MilA is a potential critical amino acid anchoring one molecule of water for hydroxylation. Thr102 of MilA is predicted as potential critical amino acid anchoring one molecule of water for hydroxylation Streptomyces rimofaciens ?
-
?
additional information 5-hydroxymethylcytosine is present in a nucleoside antibiotic mildiomycin and its formation is governed by a cytidylate hydroxymethylase MilA Streptomyces rimofaciens ZJU5119 ?
-
?
additional information MilA uses solvent water as the hydroxyl group donor like cytidylate hydroxymethylase. Thr102 of MilA is a potential critical amino acid anchoring one molecule of water for hydroxylation. Thr102 of MilA is predicted as potential critical amino acid anchoring one molecule of water for hydroxylation Streptomyces rimofaciens ZJU5119 ?
-
?

Synonyms

Synonyms Comment Organism
cytidylate hydroxymethylase
-
Streptomyces rimofaciens
MilA
-
Streptomyces rimofaciens

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Streptomyces rimofaciens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
assay at Streptomyces rimofaciens

Cofactor

Cofactor Comment Organism Structure
5,10-methylenetetrahydrofolate
-
Streptomyces rimofaciens

General Information

General Information Comment Organism
evolution since MilA have similar mechanism as CH in hydroxyl group formation, it may belong to the superfamily of thymidylate synthase and cytidylate hydroxymethylase Streptomyces rimofaciens
metabolism mildiomycin formation pathway catalyzed by MilA and MilB, overview Streptomyces rimofaciens
additional information six homologous ORFs originally annotated as putative thymidylate synthase are more likely to be CMP hydroxymethylase Streptomyces rimofaciens
physiological function several nucleotide-derived nucleoside antibiotics feature modified bases such as hydroxymethyl pyrimidine in polyoxin, and hydroxymethyl cytosine in mildiomycin. The CMP hydroxymethylase named MilA in the biosynthetic pathway of nucleoside mildiomycin in Streptoverticillum rimofaciens ZJU5119 can convert CMP in vitro in the presence of tetrahydrofolate to 5-hydroxymethyl-CMP that is immediately hydrolyzed into free 5-hydroxymethylcytosine by MilB Streptomyces rimofaciens