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PDBsum entry 6itd
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Oxidoreductase
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PDB id
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6itd
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References listed in PDB file
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Key reference
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Title
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A suicide enzyme catalyzes multiple reactions for biotin biosynthesis in cyanobacteria.
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Authors
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K.Sakaki,
K.Ohishi,
T.Shimizu,
I.Kobayashi,
N.Mori,
K.Matsuda,
T.Tomita,
H.Watanabe,
K.Tanaka,
T.Kuzuyama,
M.Nishiyama.
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Ref.
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Nat Chem Biol, 2020,
16,
415-422.
[DOI no: ]
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PubMed id
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Abstract
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In biotin biosynthesis, the conversion of pimeloyl intermediates to biotin is
catalyzed by a universal set of four enzymes: BioF, BioA, BioD and BioB. We
found that the gene homologous to bioA, the product of which is involved in the
conversion of 8-amino-7-oxononanoate (AON) to 7,8-diaminononanoate (DAN), is
missing in the genome of the cyanobacterium Synechocystis sp. PCC 6803. We
provide structural and biochemical evidence showing that a novel dehydrogenase,
BioU, is involved in biotin biosynthesis and functionally replaces BioA. This
enzyme catalyzes three reactions: formation of covalent linkage with AON to
yield a BioU-DAN conjugate at the ε-amino group of Lys124 of BioU using
NAD(P)H, carboxylation of the conjugate to form BioU-DAN-carbamic acid, and
release of DAN-carbamic acid using NAD(P)+. In this biosynthetic
pathway, BioU is a suicide enzyme that loses the Lys124 amino group after a
single round of reaction.
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