2.1.1.107: uroporphyrinogen-III C-methyltransferase

This is an abbreviated version!
For detailed information about uroporphyrinogen-III C-methyltransferase, go to the full flat file.

Reaction

2 S-adenosyl-L-methionine +

Synonyms

adenosylmethionine-uroporphyrinogen III methyltransferase, At5g40850, CobA, CobA/HemD, CysG, HemD-CobA, NirE, S-adenosyl-L-methionine dependent uroporphyrinogen III methylase, S-adenosyl-L-methionine-dependent uroporphyrinogen III methyltransferase, S-adenosyl-L-methionine: uroporphyrinogen III methyltransferase, S-adenosyl-L-methionine:uroporphyrinogen III methyltransferase, SAM-dependent uroporphyrinogen III methyltransferase, sirohaem synthase, SUMT, UMT, UPM1, UroM, uroporphyrinogen III C-methyltransferase, uroporphyrinogen III methylase, uroporphyrinogen III methyltransferase, uroporphyrinogen III methyltransferase/synthase, uroporphyrinogen III synthase/methyltransferase, uroporphyrinogen methyltransferase,

ECTree

     2 Transferases

         2.1 Transferring one-carbon groups

             2.1.1 Methyltransferases

                2.1.1.107 uroporphyrinogen-III C-methyltransferase

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Results	in table
37557	AA Sequence
2	Application
1	CAS Registry Number
21	Cloned(Commentary)
5	Cofactor
4	Crystallization (Commentary)
1	Expression
8	General Information
1	General Stability
7	Inhibitors
1	Ki Value [mM]
8	KM Value [mM]
4	Localization
1	Metals/Ions
27	Molecular Weight [Da]
24	Natural Substrates/ Products (Substrates)
33	Organism
6	Pathway
50	PDB ID
3	pH Optimum
33	Protein Variants
12	Purification (Commentary)
3	Reaction
1	Reaction Type
32	Reference
3	Source Tissue
6	Specific Activity [micromol/min/mg]
1	Storage Stability
55	Substrates and Products (Substrate)
17	Subunits
40	Synonyms
1	Systematic Name
2	Temperature Optimum [°C]
1	Temperature Stability [°C]
1	Turnover Number [1/s]

Crystallization

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Crystallization on EC 2.1.1.107 - uroporphyrinogen-III C-methyltransferase

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

atomistic molecular dynamics study. The binding of the substrate contributes to the stabilization of the structure of the full complex. Conformational changes influence the orientation of the pyrrole rings in the substrate. Conformotional motions lead to more open conformation of enzyme active site to accommodate the substrate

Pseudomonas aeruginosa

P95417

758359

sitting drop vapor diffusion method, using Tris, pH 8.0, 24% (w/v) PEG 6000 for enzyme without substrate, and 0.2 M lithium sulfate, 0.1 M Tris, pH 8.5, 1.26 M ammonium sulfate for enzyme in complex with uroporphyrinogen III

Pseudomonas aeruginosa

P95417

719948

enzyme topology diagramm

Pseudomonas denitrificans (nom. rej.)

-

662638

both apoform and with S-adenosyl-L-methionine

Thermus thermophilus

-

660612