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Literature summary for 2.1.1.107 extracted from

  • Lobo, S.A.; Brindley, A.; Warren, M.J.; Saraiva, L.M.
    Functional characterization of the early steps of tetrapyrrole biosynthesis and modification in Desulfovibrio vulgaris Hildenborough (2009), Biochem. J., 420, 317-325.
    View publication on PubMed
Search for more literature for 2.1.1.107

Cloned(Commentary)

Cloned (Comment) Organism
DNA and amino acid sequence determination and analysis, the uroporphyrinogen III synthase is naturally fused with the methyltransferase, bypassing the need for uroporphyrinogen III decarboxylase activity, overview. Expression of cobA/hemD and isolate hemD or cobA in Escherichia coli strain BL21(DE3) Desulfovibrio vulgaris

Protein Variants

Protein Variants Comment Organism
additional information separation of the individual enzyme activities, uroporphyrinogen III synthase and uroporphyrinogen III methyltransferase, by dissecting the relevant gene to allow the production of two distinct proteins Desulfovibrio vulgaris

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0004
-
 uroporphyrinogen III pH 8.0, 22°C, CobA/HemD Desulfovibrio vulgaris

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
55000
-
 x * 55000, about, recombinant CobA/HemD, SDS-PAGE Desulfovibrio vulgaris

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Desulfovibrio vulgaris uroporphyrinogen III synthase is fused to uroporphyrinogen III methyltransferase in Desulfovibrio vulgaris ?
-
 ?
uroporphyrinogen III + S-adenosyl-L-methionine Desulfovibrio vulgaris via precorrin-1 precorrin-2 + S-adenosyl-L-homocysteine
-
 ?

Organism

Organism UniProt Comment Textmining
Desulfovibrio vulgaris
-
 gene cobA/hemD
-

Purification (Commentary)

Purification (Comment) Organism
recombinant CobA/HemD , HemD, and CobA from Escherichia coli strain BL21(DE3) by nickel affinity chromatography Desulfovibrio vulgaris

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.003
-
 purified recombinant CobA/HemD Desulfovibrio vulgaris

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information uroporphyrinogen III synthase is fused to uroporphyrinogen III methyltransferase in Desulfovibrio vulgaris Desulfovibrio vulgaris ?
-
 ?
uroporphyrinogen III + S-adenosyl-L-methionine via precorrin-1 Desulfovibrio vulgaris precorrin-2 + S-adenosyl-L-homocysteine
-
 ?

Subunits

Subunits Comment Organism
? x * 55000, about, recombinant CobA/HemD, SDS-PAGE Desulfovibrio vulgaris

Synonyms

Synonyms Comment Organism
HemD-CobA
-
 Desulfovibrio vulgaris
uroporphyrinogen III methyltransferase/synthase
-
 Desulfovibrio vulgaris

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
22
-
 assay at room temperature Desulfovibrio vulgaris

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
 assay at Desulfovibrio vulgaris

Cofactor

Cofactor Comment Organism Structure
S-adenosyl-L-methionine
-
 Desulfovibrio vulgaris

General Information

General Information Comment Organism
metabolism the enzyme is involved in the tetrapyrrole biosynthesis. Uroporphyrinogen III represents the first branch point in the pathway, where the action of enzymes such as HemE, F (N) and G results in the formation of protoporphyrin IX, a precursor of modified tetrapyrroles such as haem and chlorophyll. Alternatively, uroporphyrinogen III can undergo a S-adenosylmethionine-dependent transmethylation positions 2 and 7, by CysG, Met1p or CobA depending on the organism, to generate precorrin-2, a highly unstable yellow dipyrrocorphin, overview Desulfovibrio vulgaris