Abstract
Previously, the E. coli cysG gene product had been shown to sequentially methylate uro'gen III to produce precorrin-2, hence it was given the trivial name uro'gen III methylase. We now report that in addition to methylase activity, the CysG protein catalyses both the NAD+ dependent oxidation of precorrin-2 to sirohydrochlorin, but also the insertion of iron into this oxidized intermediate, thereby producing siroheme. Thus CysG is a multifunctional protein solely responsible for siroheme synthesis from uro'gen III in E. coli, and accordingly is renamed siroheme synthase.
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Sequence
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Binding Sites
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Escherichia coli / enzymology
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Escherichia coli / genetics*
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Genes, Bacterial*
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Heme / analogs & derivatives
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Heme / biosynthesis
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Magnetic Resonance Spectroscopy
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Methylation
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Methyltransferases / chemistry
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Methyltransferases / genetics*
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Methyltransferases / metabolism
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Molecular Sequence Data
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Multienzyme Complexes / chemistry
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Multienzyme Complexes / genetics*
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Multienzyme Complexes / metabolism
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NAD / metabolism
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NAD / pharmacology
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Sequence Homology, Amino Acid
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Uroporphyrinogens / metabolism
Substances
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Multienzyme Complexes
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Uroporphyrinogens
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NAD
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Heme
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siroheme
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Methyltransferases
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uroporphyrin-III C-methyltransferase