We found a match
Your institution may have access to this item. Find your institution then sign in to continue.
- Title
Discovery of a RuBisCO-like Protein that Functions as an Oxygenase in the Novel D-Hamamelose Pathway.
- Authors
Kim, Suk Min; Lim, Hyun Seung; Lee, Sun Bok
- Abstract
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.
- Subjects
BIOCHEMISTRY; MOLECULAR biology; CHEMICAL reactions; RIBULOSE bisphosphate carboxylase; BIOSYNTHESIS; OXYGENASES; PROTEINS
- Publication
Biotechnology & Bioprocess Engineering, 2018, Vol 23, Issue 5, p490
- ISSN
1226-8372
- Publication type
Article
- DOI
10.1007/s12257-018-0305-6