Pipecolic acid in microbes: Biosynthetic routes and enzymes

Journal of Industrial Microbiology and Biotechnology

Volumn 33, Issue 6, 2006, Pages 401-407

  He, Min ^a  

^a WYETH RESEARCH   (United States)

Author keywords

Biosynthesis; Lysine metabolism; Microbial secondary metabolites; Pipecolic acid

Indexed keywords

2 AMINOADIPIC ACID; MARCFORTINE A; PIPECOLIC ACID; RAPAMYCIN; SLAFRAMINE; SWAINSONINE; TACROLIMUS; UNCLASSIFIED DRUG; VIRGINIAMYCIN S;

BIOGENESIS; BIOLOGICAL ACTIVITY; BIOSYNTHESIS; ENZYME MECHANISM; ENZYME SYNTHESIS; METABOLITE; MICROBIAL METABOLISM; MUTATION; NONHUMAN; PSEUDOMONAS PUTIDA; REVIEW; STRUCTURE ACTIVITY RELATION;

2-AMINOADIPIC ACID; BACTERIA; LYSINE; PIPECOLIC ACIDS;

PSEUDOMONAS PUTIDA;

EID: 33646446311     PISSN: 13675435     EISSN: 14765535     Source Type: Journal    
DOI: 10.1007/s10295-006-0078-3     Document Type: Review

References (56)

1. Broquist HP (1991) Lysine-pipecolic acid metabolic relationships in microbes and mammals. Annu Rev Nutr 11:435-448
2. Gupta RN, Spenser ID (1969) Biosynthesis of the piperidine nucleus. The mode of incorporation of lysine into pipecolic acid and into piperidine alkaloids. J Biol Chem 244:88-94
3. Chang YF, Adams E (1974) D-Lysine catabolic pathway in Pseudomonas putida: interrelations with L-lysine catabolism. J Bacteriol 117:753-764
4. Chang YF, Adams E (1971) Induction of separate catabolic pathways for L- and D-lysine in Pseudomonas putida. Biochem Biophys Res Commun 45:570-577
5. Fothergill JC, Guest JR (1977) Catabolism of L-lysine by Pseudomonas aeruginosa. J Gen Microbiol 99:139-155
6. Miller DL, Rodwell VW (1971) Metabolism of basic amino acids in Pseudomonas putida. Catabolism of lysine by cyclic and acyclic intermediates. J Biol Chem 246:2758-2764
7. 1-piperideine-2-carboxylate reductase of Pseudomonas putida. J Bacteriol 149:864-871
8. 1-piperideine-2-carboxylate/delta1-pyrroline- 2-carboxylate reductase involved in the catabolism of D-lysine and D-proline. J Biol Chem 280:5329-5335
9. Yonaha K, Misono H, Yamamoto T, Soda K (1975) D-Amino acid aminotransferase of Bacillus sphaericus: enzymologic and spectrometric properties. J Biol Chem 250:6983-6989
10. Kusakabe H, Kodama K, Kuninaka A, Yoshino H, Misono H, Soda K (1980) A new antitumor enzyme, L-lysine α-oxidase from Trichoderma viride. Purification and enzymological properties. J Biol Chem 255:976-981
11. Lukasheva EV, Berezov TT (2002) L-Lysine α-oxidase: physicochemical and biological properties. Biochemistry (Moscow) 67:1152-1158
12. Bruntner C, Bormann C (1998) The Streptomyces tendae Tu901 L-lysine 2-aminotransferase catalyzes the initial reaction in nikkomycin D biosynthesis. Eur J Biochem 254:347-355
13. Jordan B, Schmidt RM, Pape H (1984) Nikkomycin formation and lysine metabolism in Streptomyces tendae. In: The 3rd European congress on biotechnology. 1:451-455. Verlag Chemie, Weinheim
14. Cardenas ME, Zhu D, Heitman J (1995) Molecular mechanisms of immunosuppression by cyclosporine, FK506, and rapamycin. Curr Opin Nephrol Hypertens 4:472-477
15. Sanglier JJGB, Dreyfuss M, Fehr T, Traber R, Schreier MH (1993) Immunosuppressants of microbial origin, Developments in industrial microbiology series, vol. 32. Wm, C. Brown Publisher, Dubuque, pp 1-27
16. Paiva NL, Demain AL, Roberts MF (1993) The immediate precursor of the nitrogen-containing ring of rapamycin is free pipecolic acid. Enzyme Microb Technol 15:581-585
17. Banaszynski LA, Liu, CW, Wandless TJ (2005) Characterization of the FKBP.rapamycin.FRB ternary complex. J Am Chem Soc 127:4715-4721
18. Choi J, Chen J, Schreiber SL, Clardy J (1996) Structure of the FKBP12-rapamycin complex interacting with the binding domain of human FRAP. Science 273:239-242
19. Meadows RP, Nettesheim DG, Xu RX, Olejniczak ET, Petros AM, Holzman TF, Severin J, Gubbins E, Smith H, Fesik SW (1993) Three-dimensional structure of the FK506 binding protein/ascomycin complex in solution by heteronuclear three-and four-dimensional NMR. Biochemistry 32:754-765
20. Byrne KM, Shafiee A, Nielsen J, Arison B, Monaghan RL, Kaplan L (1993) The biosynthesis and enzymology of an immunosuppressant, immunomycin, produced by Streptomyces hygroscopicus var. ascomyceticus. Dev Ind Microbiol 32:29-45
21. Molnar I, Aparicio JF, Haydock SF, Khaw LE, Schwecke T, Konisg A, Staunton J, Leadlay PF (1996) Organization of the biosynthetic gene cluster for rapamycin in Streptomyces hygroscopicus: analysis of genes flanking the polyketide synthase. Gene 169:1-7
22. Schwecke T, Aparicio JF, Molnar I, Konig A, Khaw LE, Haydock SF, Oliynyk M, Caffrey P, Cortes J, Lester JB et al (1995) The biosynthetic gene cluster for the polyketide immunosuppressant rapamycin. Proc Natl Acad Sci USA 92:7839-7843
23. Sans N, Schindler U, Schroder J (1988) Ornithine cyclodeaminase from Ti plasmid C58: DNA sequence, enzyme properties and regulation of activity by arginine. Eur J Biochem 173:123-130
24. Schindler U, Sans N, Schroder J (1989) Ornithine cyclodeaminase from octopine Ti plasmid Ach5: identification, DNA sequence, enzyme properties, and comparison with gene and enzyme from nopaline Ti plasmid C58. J Bacteriol 171:847-854
25. Khaw LE, Bohm GA, Metcalfe S, Staunton J, Leadlay PF (1998) Mutational biosynthesis of novel rapamycins by a strain of Streptomyces hygroscopicus NRRL 5491 disrupted in rapL, encoding a putative lysine cyclodeaminase. J Bacteriol 180:809-814
26. Motamedi H, Shafiee A (1998) The biosynthetic gene cluster for the macrolactone ring of the immunosuppressant FK506. Eur J Biochem 256:528-534
27. Wu K, Chung L, Revill WP, Katz L, Reeves CD (2000) The FK520 gene cluster of Streptomyces hygroscopicus var. ascomyceticus (ATCC 14891) contains genes for biosynthesis of unusual polyketide extender units. Gene 251:81-90
28. Muth WL, Costilow RN (1974) Ornithine cyclase (deaminating). III. Mechanism of the conversion of ornithine to proline. J Biol Chem 249:7463-7467
29. Namwat W, Kamioka Y, Kinoshita H, Yamada Y, Nihira T (2002) Characterization of virginiamycin S biosynthetic genes from Streptomyces virginiae. Gene 286:283-290
30. Paris JM, Barriere JC, Smith C, Bost PE (1990) The chemistry of pristinamycins. Recent progress in the chemical synthesis of antibiotics. Springer, Berlin Heidelberg New York, pp 183-248
31. Yamada Y, Nihira T, Sakuda S (1997) Butyrolactone autoregulators, inducers of virginiamycin in Streptomyces virginiae: their structures, biosynthesis, recepter proteins, and induction of virginiamycin biosynthesis. In: Strolhl WR (ed) Biotechnology of antibiotics. Marcel Dekker, New York, pp 63-79
32. Molinero AA, Kingston DGI, Reed JW (1989) Biosynthesis of antibiotics of the virginiamycin family. 6. Biosynthesis of virginiamycin S1. J Nat Prod 52:99-108
33. Reed JW, Purvis MB, Kingston DGI, Biot A, Gossele F (1989) Biosynthesis of antibiotics of the virginiamycin family. 7. Stereo-and regiochemical studies on the formation of the 3-hydroxypicolinic acid and pipecolic acid units. J Org Chem 54:1161-1165
34. Namwat W, Kinoshita H, Nihira T (2002) Identification by heterologous expression and gene disruption of VisA as L-lysine 2-aminotransferase essential for virginiamycin S biosynthesis in Streptomyces virginiae. J Bacteriol 184:4811-4818
35. Broquist HP (1985) The indolizidine alkaoids, slaframine and swainsonine: contaminants in animal forages. Annu Rev Nutr 5:391-409
36. 1-piperideine-6-carboxylic acid pathway. J Biol Chem 265:14742-14747
37. Wickwire BM, Wagner C, Broquist HP (1990) Pipecolic acid biosynthesis in Rhizoctonia leguminicola. II. Saccharopine oxidase: a unique flavin enzyme involved in pipecolic acid biosynthesis. J Biol Chem 265:14748-14753
38. Kinzel JJ, Bhattacharjee JK (1979) Role of pipecolic acid in the biosynthesis of lysine in Rhodotorula glutinis. J Bacteriol 138:410-417
39. Kurtz M, Bhattacharjee JK (1975) Biosynthesis of lysine in Rhodotorula glutinis: role of pipecolic acid. J Gen Microbiol 86:103-110
40. Rius N, Demain AL (1997) Lysine ε-aminotransferase, the initial enzyme of cephalosporin biosynthesis in actinomycetes. J Microbiol Biotechnol 7:95-100
41. Aharonowitz Y, Cohen G, Martin JF (1992) Penicillin and cephalosporin biosynthetic genes: structure, organization, regulation, and evolution. Annu Rev Microbiol 46:461-495
42. Tobin MB, Kovacevic S, Madduri K, Hoskins JA, Skatrud PL, Vining LC, Stuttard C, Miller JR (1991) Localization of the lysine ε-aminotransferase (lat) and Δ-(L-α-aminoadipyl)-L-cysteinyl-D-valine synthetase (pcbAB) genes from Streptomyces clavuligerus and production of lysine ε-aminotransferase activity in Escherichia coli. J Bacteriol 173:6223-6229
43. Madduri K, Stuttard C, Vining LC (1989) Lysine catabolism in Streptomyces spp. is primarily through cadaverine: β-lactam producers also make α-aminoadipate. J Bacteriol 171:299-302
44. Fujii T, Narita T, Agematu H, Agata N, Isshiki K (2000) Characterization of L-lysine 6-aminotransferase and its structural gene from Flavobacterium lutescens IFO3084. J Biochem 128:391-397
45. 1- piperideine-6-carboxylic acid. Biochemistry 7:4102-4109
46. Fujii T, Mukaihara M, Agematu H, Tsunekawa H (2002) Biotransformation of L-lysine to L-pipecolic acid catalyzed by L-lysine 6-aminotransferase and pyrroline-5-carboxylate reductase. Biosci Biotechnol Biochem 66:622-627
47. Fujii T, Aritoku Y, Agematu H, Tsunekawa H (2002) Increase in the rate of L-pipecolic acid production using lat-expressing Escherichia coli by lysP and yeiE amplification. Biosci Biotechnol Biochem 66:1981-1984
48. 1- pyrroline-5-carboxylate reductase. J Bacteriol 174:3782-3788
49. 1- pyrroline-5-carboxylate reductase was isolated by functional complementation in Escherichia coli and is found to be osmoregulated. Mol Gen Genet 221:299-305
50. Leisinger T (1987) Biosynthesis of proline. In: Neidhardt FC, Ingraham JL, Low KB, Magasanic B, Schaechter M, Umbarger HE (eds) Escherichia coli and Salmonella typhimurium: cellular and molecular biology. American Society for Microbiology, Washington, pp 345-351
51. Smith RJ, Downing SJ, Phang JM, Lodato RF, Aoki TT (1980) Pyrroline-5-carboxylate reductase activity in mammalian cells. Proc Natl Acad Sci USA 77:5221-5225
52. Aspen AJ, Meister A (1962) Conversion of α-aminoadipic acid to L-pipecolic acid by Aspergillus nidulans. Biochemistry 1:606-612
53. Casqueiro J, Bañuelos O, Sutiérrez S, Martín JF (2001) Metabolic engineering of the lysine pathway for β-lactam over-production in Penicillium chrysogenum. In: Van Broedkhoven A, Anne J, Shapiro F (eds) Focus on biotechnology, vol.1. Novel frontiers in the production of compounds for biomedical use. Kluwer Academic Publishers, Dordrecht, pp 147-159
54. Naranjo L, Martin de Valmaseda E, Banuelos O, Lopez P, Riano J, Casqueiro J, Martin JF (2001) Conversion of pipecolic acid into lysine in Penicillium chrysogenum requires pipecolate oxidase and saccharopine reductase: characterization of the lys7 gene encoding saccharopine reductase. J Bacteriol 183:7165-7172
55. Naranjo L, Martin de Valmaseda E, Casqueiro J, Ullan RV, Lamas-Maceiras M, Banuelos O, Martin JF (2004) Inactivation of the lys7 gene, encoding saccharopine reductase in Penicillium chrysogenum, leads to accumulation of the secondary metabolite precursors piperideine-6-carboxylic acid and pipecolic acid from α-aminoadipic acid. Appl Environ Microbiol 70:1031-1039
56. Kuo MS, Yurek DA, Mizsak SA, Cialdella JI, Baczynskyj L, Marshall VP (1999) Biosynthesis of the pipecolate moiety of marcfortine A. J Am Chem Soc 121:1763-1767