l-Leucine 5-hydroxylase of Nostoc punctiforme is a novel type of Fe(II)/α-ketoglutarate-dependent dioxygenase that is useful as a biocatalyst
- 967 Downloads
l-Leucine 5-hydroxylase (LdoA) previously found in Nostoc punctiforme PCC 73102 is a novel type of Fe(II)/α-ketoglutarate-dependent dioxygenase. LdoA catalyzed regio- and stereoselective hydroxylation of l-leucine and l-norleucine into (2S,4S)-5-hydroxyleucine and (2S)-5-hydroxynorleucine, respectively. Moreover, LdoA catalyzed sulfoxidation of l-methionine and l-ethionine in the same manner as previously described l-isoleucine 4-hydroxylase. Therefore LdoA should be a promising biocatalyst for effective production of industrially useful amino acids.
Keywordsl-Leucine 5-hydroxylase Fe(II)/α-ketoglutarate-dependent dioxygenase (2S,4S)-5-Hydroxyleucine (2S)-5-Hydroxynorleucine Nostocyclopeptide
This work was partially supported by Grants-in-Aid for Scientific Research (no. 21780070 and 24688010 to M. Hibi, and no. 22658027 and 23248014 to J. Ogawa) from the Ministry of Education, Culture, Sports, Science and Technology of Japan.
- Broca C, Gross R, Petit P, Sauvaire Y, Manteghetti M, Tournier M, Masiello P, Gomis R, Ribes G (1999) 4-Hydroxyisoleucine: experimental evidence of its insulinotropic and antidiabetic properties. Am J Physiol Endocrinol Metab 277:40–44Google Scholar
- Ford PW, Gustafson KR, McKee TC, Shigematsu N, Maurizi LK, Pannell LK, Williams DE, De Silva ED, Lassota P, Allen TM, Van Soest R, Andersen RJ, Boyd MR (1999) Papuamides A-D, HIV-inhibitory and cytotoxic depsipeptides from the sponges Theonella mirabilis and Theonella swinhoei collected in Papua New Guinea. J Am Chem Soc 121:5899–5909CrossRefGoogle Scholar
- Kodera T, Smirnov SV, Samsonova NN, Kozlov YI, Koyama R, Hibi M, Ogawa J, Yokozeki K, Shimizu S (2009) A novel l-isoleucine hydroxylating enzyme, l-isoleucine dioxygenase from Bacillus thuringiensis, produces (2S,3R,4S)-4-hydroxyisoleucine. Biochem Biophys Res Commun 390:506–510CrossRefGoogle Scholar
- Mori H, Shibasaki T, Yano K, Ozaki A (1997) Purification and cloning of a proline 3-hydroxylase, a novel enzyme which hydroxylates free l-proline to cis-3-hydroxy-L-proline. J Bacteriol 179:5677–5683Google Scholar
- Ogawa J, Yamanaka H, Mano J, Doi Y, Horinouchi N, Kodera T, Nio N, Smirnov SV, Samsonova NN, Kozlov YI, Shimizu S (2007) Synthesis of 4-hydroxyisoleucine by the aldolase-transaminase coupling reaction and basic characterization of the aldolase from Arthrobacter simplex AKU 626. Biosci Biotechnol Biochem 71:1607–1615CrossRefGoogle Scholar
- Ogawa J, Kodera T, Smirnov SV, Hibi M, Samsonova NN, Koyama R, Yamanaka H, Mano J, Kawashima T, Yokozeki K, Shimizu S (2011) A novel l-isoleucine metabolism in Bacillus thuringiensis generating (2S,3R,4S)-4-hydroxyisoleucine, a potential insulinotropic and anti-obesity amino acid. Appl Microbiol Biotechnol 89:1929–1938CrossRefGoogle Scholar
- Ota Y, Gomi S, Yanai K (2008) Novel protein having l-leucine hydroxylase activity, useful for producing 2S,4S-5-hydroxy leucine for producing useful substance such as pharmaceutical. International Patent Application WO2008013262-A1; JP2008526830-XGoogle Scholar
- Rippka R, Deruelles J, Waterbury JB (1979) Generic assignments, strain histories and properties of pure cultures of cyanobacteria. J Gen Microbiol 111:1–61Google Scholar
- Shibasaki T, Mori H, Chiba S, Ozaki A (1999) Microbial proline 4-hydroxylase screening and gene cloning. Appl Environ Microbiol 65:4028–4031Google Scholar
- Smirnov SV, Samsonova NN, Novikova AE, Matrosov NG, Rushkevich NY, Kodera T, Ogawa J, Yamanaka H, Shimizu S (2007) A novel strategy for enzymatic synthesis of 4-hydroxyisoleucine: identification of an enzyme possessing HMKP (4-hydroxy-3-methyl-2-keto-pentanoate) aldolase activity. FEMS Microbiol Lett 273:70–77CrossRefGoogle Scholar