In Saccharomyces cerevisiae, the last two steps are carried out by a single bifunctional enzyme, Met8p.
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| rdf:type | |
| rdfs:comment |
Also involved in the biosynthesis of cobalamin.,
In Saccharomyces cerevisiae, the last two steps are carried out by a single bifunctional enzyme, Met8p.,
In some bacteria, steps 1-3 are catalyzed by a single multifunctional protein called CysG, whereas in Bacillus megaterium, three separate enzymes carry out each of the steps, with SirA being responsible for the above reaction.,
It is the first of three steps leading to the formation of siroheme from uroporphyrinogen III.,
The second step involves an NAD(+)-dependent dehydrogenation to form sirohydrochlorin from precorrin-2 (EC 1.3.1.76) and the third step involves the chelation of Fe(2+) to sirohydrochlorin to form siroheme (EC 4.99.1.4).,
This enzyme catalyzes two sequential methylation reactions, the first forming precorrin-1 and the second leading to the formation of precorrin-2.
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| rdfs:subClassOf | |
| skos:broaderTransitive | |
| uniprot:name |
Adenosylmethionine-uroporphyrinogen III methyltransferase,
S-adenosyl-L-methionine-dependent uroporphyrinogen III methylase,
SUMT,
Urogen III methylase,
Uroporphyrin-III C-methyltransferase,
Uroporphyrinogen III methylase,
Uroporphyrinogen methyltransferase,
Uroporphyrinogen-III C-methyltransferase,
Uroporphyrinogen-III methylase,
Uroporphyrinogen-III methyltransferase
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| uniprot:activity |
(1) S-adenosyl-L-methionine + uroporphyrinogen III = S-adenosyl-L-homocysteine + precorrin-1.,
(2) S-adenosyl-L-methionine + precorrin-1 = S-adenosyl-L-homocysteine + precorrin-2.
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