Uroporphyrinogen-III C-methyltransferase
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Uroporphyrinogen-III C-methyltransferase (), ''uroporphyrinogen methyltransferase'', ''uroporphyrinogen-III methyltransferase'', ''adenosylmethionine-uroporphyrinogen III methyltransferase'', ''S-adenosyl-L-methionine-dependent uroporphyrinogen III methylase'', ''uroporphyrinogen-III methylase'', ''SirA'', ''CysG'', ''CobA'', ''uroporphyrin-III C-methyltransferase'', ''S-adenosyl-L-methionine:uroporphyrin-III C-methyltransferase'') is an
enzyme An enzyme () is a protein that acts as a biological catalyst by accelerating chemical reactions. The molecules upon which enzymes may act are called substrate (chemistry), substrates, and the enzyme converts the substrates into different mol ...
with
systematic name A systematic name is a name given in a systematic way to one unique group, organism, object or chemical substance, out of a specific population or collection. Systematic names are usually part of a nomenclature. A semisystematic name or semitrivi ...
''S-adenosyl-L-methionine:uroporphyrinogen-III C-methyltransferase''. This enzyme catalyses the following
chemical reaction A chemical reaction is a process that leads to the chemistry, chemical transformation of one set of chemical substances to another. When chemical reactions occur, the atoms are rearranged and the reaction is accompanied by an Gibbs free energy, ...
: 2
S-adenosyl-L-methionine ''S''-Adenosyl methionine (SAM), also known under the commercial names of SAMe, SAM-e, or AdoMet, is a common cosubstrate involved in methyl group transfers, transsulfuration, and aminopropylation. Although these anabolic reactions occur throug ...
+ uroporphyrinogen III \rightleftharpoons 2 S-adenosyl-L-homocysteine + precorrin-2 (overall reaction) :(1a) S-adenosyl-L-methionine + uroporphyrinogen III \rightleftharpoons S-adenosyl-L-homocysteine + precorrin-1 :(1b) S-adenosyl-L-methionine + precorrin-1 \rightleftharpoons S-adenosyl-L-homocysteine + precorrin-2 Uroporphyrinogen-III C-methyltransferase catalyses two
methylation Methylation, in the chemistry, chemical sciences, is the addition of a methyl group on a substrate (chemistry), substrate, or the substitution of an atom (or group) by a methyl group. Methylation is a form of alkylation, with a methyl group replac ...
reactions. The first reaction converts
uroporphyrinogen III Uroporphyrinogen III is a tetrapyrrole, the first macrocycle, macrocyclic intermediate in the biosynthesis of heme, chlorophyll, vitamin B12, and siroheme. It is a colorless compound, like other porphyrinogens. Structure The molecular structure of ...
into precorrin-1. The second converts precorrin-1 into precorrin-2. These reactions are part of the biosynthetic pathway to
cobalamin Vitamin B12, also known as cobalamin, is a water-soluble vitamin involved in metabolism. One of eight B vitamins, it serves as a vital cofactor (biochemistry), cofactor in DNA synthesis and both fatty acid metabolism, fatty acid and amino a ...
(vitamin B12) in both
anaerobic Anaerobic means "living, active, occurring, or existing in the absence of free oxygen", as opposed to aerobic which means "living, active, or occurring only in the presence of oxygen." Anaerobic may also refer to: *Adhesive#Anaerobic, Anaerobic ad ...
and
aerobic Aerobic means "requiring air," in which "air" usually means oxygen. Aerobic may also refer to * Aerobic exercise, prolonged exercise of moderate intensity * Aerobics, a form of aerobic exercise * Aerobic respiration, the aerobic process of cellu ...
bacteria Bacteria (; : bacterium) are ubiquitous, mostly free-living organisms often consisting of one Cell (biology), biological cell. They constitute a large domain (biology), domain of Prokaryote, prokaryotic microorganisms. Typically a few micr ...
.


See also

*
Cobalamin biosynthesis Cobalamin biosynthesis is the process by which bacteria and archea make Vitamin B12, cobalamin, vitamin B12. Many steps are involved in converting aminolevulinic acid via uroporphyrinogen III and adenosylcobyric acid to the final forms in which i ...


References


External links

* {{Portal bar, Biology, border=no EC 2.1.1