TY - JOUR
T1 - A suicide enzyme catalyzes multiple reactions for biotin biosynthesis in cyanobacteria
AU - Sakaki, Kei
AU - Ohishi, Keita
AU - Shimizu, Tetsu
AU - Kobayashi, Ikki
AU - Mori, Naoki
AU - Matsuda, Kenichi
AU - Tomita, Takeo
AU - Watanabe, Hidenori
AU - Tanaka, Kan
AU - Kuzuyama, Tomohisa
AU - Nishiyama, Makoto
N1 - Funding Information:
This work was supported in part by JSPS KAKENHI (grant no. 17H06168 to M.N.) and the Research Committee of B group Vitamins (to M.N.). We are grateful to the staff at Photon Factory for their assistance with data collection, which was approved by the Photon Factory Program Advisory Committee (proposals nos. 2015G546, 2017G574 and 2019G548).
Publisher Copyright:
© 2020, The Author(s), under exclusive licence to Springer Nature America, Inc.
PY - 2020/4/1
Y1 - 2020/4/1
N2 - 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.
AB - 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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U2 - 10.1038/s41589-019-0461-9
DO - 10.1038/s41589-019-0461-9
M3 - Article
C2 - 32042199
AN - SCOPUS:85079447223
SN - 1552-4450
VL - 16
SP - 415
EP - 422
JO - Nature Chemical Biology
JF - Nature Chemical Biology
IS - 4
ER -
