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KMID : 1094720180230050490
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Biotechnology and Bioprocess Engineering
2018 Volume.23 No. 5 p.490 ~ p.499
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Discovery of a RuBisCO-like Protein that Functions as an Oxygenase in the Novel d-Hamamelose Pathway
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Kim Suk-Min
Lim Hyun-Seung
Lee Sun-Bok
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Abstract
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Ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO) is the key catalyst of CO2 fixation in nature. RuBisCO forms I, II, and III catalyze CO2 fixation reactions, whereas form IV, also called the RuBisCO-like protein (RLP), is known to have no carboxylase or oxygenase activities. Here, we describe an RLP in Ochrobactrum anthropi ATCC 49188 (Oant_3067; HamA) that functions as an oxygenase in the metabolism of d-hamamelose, a branched-chain hexose found in most higher plants. The d-hamamelose pathway is comprised of five previously unknown enzymes: d-hamamelose dehydrogenase, d-hamamelono-lactonase, d-hamamelonate kinase, d-hamamelonate-2′,5-bisphosphate dehydrogenase (decarboxylating), and the RLP 3-keto-d-ribitol-1,5-bisphosphate (KRBP) oxygenase, which converts KRBP to 3-d-phosphoglycerate and phosphoglycolate. HamA represents the first RLP catalyzing the O2-dependent oxidative C?C bond cleavage reaction, and our findings may provide insights into its applications in oxidative cleavage of organic molecules.
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KEYWORD
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RuBisCO-like proteins, oxygenase, d-hamamelose, metabolic pathway, branched-chain sugar
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