Actinobacterial enzyme inhibitors-A review

Critical Reviews in Microbiology

Volumn 41, Issue 2, 2015, Pages 261-272

  Manivasagan, Panchanathan ^a   Venkatesan, Jayachandran ^a   Sivakumar, Kannan ^b   Kim, Se Kwon ^a  

^a Pukyong National University   (South Korea)

^b ANNAMALAI UNIVERSITY   (India)

Author keywords

Actinobacteria; Amylase inhibitors; Enzyme inhibitors; Medicine

Indexed keywords

2 EPI 5 EPIVALIOLONE; 5 OXOPROLYL PEPTIDASE INHIBITOR; ACARBOSE; ACARVIOSIN; ACARVIOSTATIN I03; ACARVIOSTATIN II03; ACARVIOSTATIN III03; ACARVIOSTATIN IV03; ALPHA GLUCOSIDASE INHIBITOR; AMYLASE INHIBITOR; ASPARTIC PROTEINASE INHIBITOR; BETA GLUCOSIDASE INHIBITOR; CHITINASE INHIBITOR; CYSTEINE PROTEINASE INHIBITOR; DIPEPTIDYL CARBOXYPEPTIDASE INHIBITOR; ENZYME INHIBITOR; EPOXOMICIN; ESTERASE INHIBITOR; METALLOPROTEINASE INHIBITOR; MIGLITOL; MONOAMINE OXIDASE INHIBITOR; N ACETYL BETA DEXTRO GLUCOSAMINIDASE INHIBITOR; PHOSPHORAMIDON; PROBESTIN; PROTEINASE INHIBITOR; SERINE PROTEINASE INHIBITOR; TENDAMISTAT; TYROSINASE INHIBITOR; UNCLASSIFIED DRUG; UNINDEXED DRUG; VALIENAMINE; BIOLOGICAL PRODUCT;

ACTINOBACTERIA; BACTERIAL STRAIN; BIOTECHNOLOGICAL PROCEDURES; DRUG STRUCTURE; ENZYME INHIBITION; HIGH THROUGHPUT SCREENING; HUMAN; INDUSTRIAL PRODUCTION; NONHUMAN; PRIORITY JOURNAL; REVIEW; SEDIMENT; STEREOCHEMISTRY; AGRICULTURE; DIAGNOSTIC TEST; DRUG THERAPY; ISOLATION AND PURIFICATION; METABOLISM; PROCEDURES;

ACTINOBACTERIA; BACTERIA (MICROORGANISMS);

ACTINOBACTERIA; AGRICULTURE; BIOLOGICAL PRODUCTS; DIAGNOSTIC TESTS, ROUTINE; DRUG THERAPY; ENZYME INHIBITORS;

EID: 84929733679     PISSN: 1040841X     EISSN: 15497828     Source Type: Journal    
DOI: 10.3109/1040841X.2013.837425     Document Type: Review

References (88)

1. Alvarez ME, White CB, Gregory J, et al. (1995). Phevalin, a new calpain inhibitor, from a Streptomyces sp. J Antibiot 48:1165-7
2. Alvarez ME, Houck DR, White CB, et al. (1994). Isolation and structure elucidation of two new calpain inhibitors from Streptomyces griseus. J Antibiot 47:1195-201
3. Aoyagi T, Hatsu M, Imada C, et al. (1992). Pyrizinostatin: a new inhibitor of pyroglutamyl peptidase. J Antibiot 45:1795-6
4. Arrieta JM, Herndl GJ. (2001). Assessing the diversity of marine bacterial b-glucosidases by capillary electrophoresis zymography. Appl Environ Microbiol 67:4896-900
5. Asano N. (2003). Glycosidase inhibitors: update and perspectives on practical use. Glycobiology 13:93R-104R
6. Asano N, Nash RJ, Molyneux RJ, Fleet GW. (2000). Sugar-mimic glycosidase inhibitors: natural occurrence, biological activity and prospects for therapeutic application. Tetrahedron Asymme. 11: 1645-80
7. Banks BJ, Haxell MA, Lunn G et al. (2007). Treatment of rumen acidosis with a-Amylase inhibitors, European Patent, EP1157696
8. Birari RB, Bhutani KK. (2007). Pancreatic lipase inhibitors from natural sources: unexplored potential. Drug Discov Today 12:879-89
9. Bo-Linn GW, Santa Ana CA, Morawski SG, Fordtran JS. (1982). Starch blockers-Their effect on calorie absorption from a high-starch meal. New Engl J Med 307:1413-16
10. Borges De Melo E, da Silveira Gomes A, Carvalho I. (2006). a-And b-Glucosidase inhibitors: chemical structure and biological activity. Tetrahedron 62:10277-302
11. Bush K, Henry PR, Souser-Woehleke M, et al. (1984). Phenacein-An angiotensin-converting enzyme inhibitor produced by a streptomycete. I. Taxonomy, fermentation and biological properties. J Antibiot 37:1308-12
12. Demuth H-U. (1990). Recent Developments in inhibiting cysteine and serine proteases. J Enzyme Inhibition Med Chem 3:249-78
13. Donkor I. (2000). A survey of calpain inhibitors. Curr Med Chem 7: 1171-88
14. Donkor I, SanDers ML. (2001). Synthesis of a reported calpain inhibitor isolated from Streptomyces griseus. Bioorg Med Chem Lett 11: 2647-9
15. Floss HG. (1997). Natural products Derived from unusual variants of the shikimate pathway. Nat Prod Rep 14:433-52
16. Friedman LS, Peterson WL. (1998). Peptic ulcer and related disorDers. In: Fauci AS, Braunwald E, Isselbacher JD, et al, eds. Harrisons principles of internal medicine. New York: McGraw-Hill, 1597-610
17. Ganesan S, Raja S, Sampathkumar P, et al. (2011). Isolation and screening of a-glucosidase enzyme inhibitor producing marine actinobacteria. Afr J Microbiol Res 5:3437-45
18. Geng P, Qiu F, Zhu Y, Bai G. (2008). Four acarviosincontaining oligosacchariDes iDentified from Streptomyces coelicoflavus ZG0656 are potent inhibitors of a-Amylase. Carbohyd Res 343: 882-92
19. Geng P, Bai G, Shi Q, et al. (2009). Taxonomy of the Streptomyces strain ZG0656 that produces acarviostatin a-Amylase inhibitors and analysis of their effects on blood glucose levels in mammalian systems. J Appl Microbiol 106:525-33
20. Hadvary P, Sidler W, Meister W, et al. (1991) the lipase inhibitor tetrahydrolipstatin binds covalently to the putative active site serine of pancreatic lipase. J Biol Chem 266:2021-7
21. Hall JE, Bhatta N, Adams JM, et al. (1991). Variable tolerance of the Developing follicle and corpus luteum to gonadotropin-releasing hormone antagonist-induced gonadotropin withdrawal in the human. J Clin Endocr Metab 72:993-1000
22. Hirayama K, Takahashi R, Akashi S, et al. (1987). Primary structure of Paim I, an alpha-Amylase inhibitor from Streptomyces corchorushii, as Determined by the combination of Edman Degradation and fast atom bombardment mass spectrometry. Biochem 26:6483-8
23. Holland D, Tronrud D, Pley H, et al. (1992). Structural comparison suggests that thermolysin and related neutral proteases unDergo hingebending motion during catalysis. Biochem 31:11310-16
24. Horovitz ZP (editor). (1981). Angiotensin converting enzyme inhibitors: mechanisms of action and clinical implications. Baltimore and Munich: Urban &Schwarzenberg
25. Imada C. (2004). Enzyme inhibitors of marine microbial origin with pharmaceutical importance. Mar Biotechnol 6:193-8
26. Imada C. (2005). Enzyme inhibitors and other bioactive compounds from marine actinomycetes. Antonie Van Leeuwenhoek 87: 59-63
27. Imada C, Okami Y. (1995). Characteristics of marine actinomycete isolated from a Deep-sea sediment and production of beta-glucosidase inhibitor. J Mar Biotechnol 2:109-13
28. Imada C, Sugimoto Y, Makimura T, et al. (2001). Isolation and characterization of tyrosinase inhibitor-producing microorganisms from marine environment. Fish Sci 67:1151-6
29. Johnston PS, Lebovitz HE, Coniff RF, et al. (1998). AdVantages of a-glucosidase inhibition as monotherapy in elDerly type 2 diabetic patients. J Clin Endocr Metab 83:1515-22
30. Kangouri K, Namiki S, Nagate T et al. (1980). Novel amylase inhibitors, US Patent, 41972921980
31. Kido Y, Hamakado T, Yoshida T, et al. (1983). Isolation and characterization of ancovenin, a new inhibitor of angiotensin I converting enzyme, produced by actinomycetes. J Antibiot 36:1295-9
32. Kim JH, Ryu YB, Kang NS, et al. (2006). Glycosidase inhibitory flavonoids from Sophora flavescens. Biol Pharm Bull 29:302-5
33. Kodani S, Ohnishi-Kameyama M, Yoshida M, Ochi K. (2011). A new siDerophore isolated from Streptomyces sp. TM-34 with potent inhibitory activity against angiotensin-converting enzyme. Eur J Org Chem 2011:3191-6
34. Krowarsch D, Cierpicki T, Jelen F, Otlewski J. (2003). Canonical protein inhibitors of serine proteases. Cell Mol Life Sci 60:2427-44
35. Kuehn L, Dahlmann B, Reinauer H. (1984). IDentification of four distinct serine proteinase inhibitors in rat skeletal muscle. Biochem Biophys Res Commun 120:96-102
36. Kunio Suetsuna, Nagatomo K, Doi K. (1994). Structure of a-Amylase inhibitor produced by marine actinomycete and its lowering effects in vivo of glucose and lipid in blood. J Shimonoseki University Fisheries 42:171-83
37. Lin G, Chattopadhyay D, Maki M, et al. (1997). Crystal structure of calcium bound domain VI of calpain at 1.9 A resolution and its role in enzyme assembly, regulation, and inhibitor binding. Nature Structural Biol 4:539-47
38. Lovejoy B, Cleasby A, Hassell AM, et al. (1994). Structure of the catalytic domain of fibroblast collagenase complexed with an inhibitor. Science 263:375-7
39. Mahmud T, Tornus I, Egelkrout E, et al. (1999). Biosynthetic studies on the a-glucosidase inhibitor acarbose in Actinoplanes sp.: 2-epi-5-epi-valiolone is the direct precursor of the valienamine moiety. J Am Chem Soc 121:6973-83
40. Manivasagan P, Venkatesan J, Sivakumar K, Kim S-K. (2013a). Actinobacterial melanins: current status and perspective for the future. World J Microbiol Biotechnol 1-14. DOI 10. 1007/s11274-013-1352-y
41. Manivasagan P, Venkatesan J, Sivakumar K, Kim S-K. (2013b). Marine actinobacterial metabolites: Current status and future perspectives. Microbiol Res 168:311-32
42. Manivasagan P, Venkatesan J, Senthilkumar K, et al. (2013c). Isolation and characterization of biologically active melanin from Actinoalloteichus sp. MA-32. Int J Biol Macromol 58:263-74
43. Meng P, Zhou X. (2012). a-Glucosidase inhibitory effect of a bioactivity guiDed fraction GIB-638 from Streptomyces fradiae PWH638 Med Chem Res 21:4422-9
44. Meng P, Xie C, Geng P, et al. (2013). Inhibitory effect of components from Streptomyces species on a-glucosidase and a-Amylase of different origin. Appl Biochem Microbiol 49:160-8
45. Menon V, Rao M. (2012). Slow-tight binding inhibition of pepsin by an aspartic protease inhibitor from Streptomyces sp. MBR04. Int J Biol Macromol 51:165-74
46. Misasa H, Matsui Y, Uehara H, et al. (1992). Tyrosinase inhibitors from Albatrellus confluens. Biosci Biotechnol Biochem 56:1660-1
47. Mutoh M, Nakada N, Matsukuma S, et al. (1994). Panclicins, novel pancreatic lipase inhibitors. I. Taxonomy, fermentation, isolation and biological activity. J Antibiot 47:1369-75
48. Oda K, Koyama T, Murao S. (1979). Purification and properties of a proteinaceous metallo-proteinase inhibitor from Streptomyces nigrescens TK-23. Biochim Biophys Acta Enzymol 571:147-56
49. Ohno A, Tate S-i, Seeram SS, et al. (1998). NMR structure of the Streptomyces metalloproteinase inhibitor, SMPI, isolated from Streptomyces nigrescens TK-23: another example of an ancestral bg-crystallin precursor structure. J Mol Biol 282:421-33
50. OnDetti MA, Rubin B, Cushman DW. (1977). Design of specific inhibitors of angiotensin-converting enzyme: new class of orally active antihypertensive agents. Science 196:441-4
51. Otto H-H, Schirmeister T. (1997). Cysteine proteases and their inhibitors. Chem Rev 97:133-72
52. Pandhare J, Zog K, DeshpanDe VV. (2002). Differential stabilities of alkaline protease inhibitors from actinomycetes: effect of various additives on thermostability. Bioresour Technol 84:165-9
53. Pierpoint W. (1966) the enzymic oxidation of chlorogenic acid and some reactions of the quinone produced. Biochem J 98:567-80
54. Powers JC, Harper JW. (1986). Inhibitors of metalloproteases. In: Barrett AJ, Salvesen G, eds. Proteinase inhibitors. Vol. 12. Amsterdam: Elsevier BV, 219-98
55. Prasad C, Peterkofsky A. (1976). Demonstration of pyroglutamylpeptidase and amidase activities toward thyrotropin-releasing hormone in hamster hypothalamus extracts. J Biol Chem 251:3229-34
56. Prashith Kekuda T, Shobha K, Onkarappa R. (2011). Pancreatic lipase inhibitory and cytotoxic potential of a Streptomyces species isolated from Western Ghat soil, Agumbe, Karnataka, India. Int J Pharmaceutical Biol Archive 2:932-7
57. Priestley G (editor). (1993). An introduction to the skin and its diseases. In: Molecular aspects of Dermatology. Vol. 1. Chichester, UK: John Wiley and Sons Ltd 17
58. Raja S, Ganesan S, Sivakumar K, Thangaradjou T. (2010). Screening of marine actinobacteria for amylase enzymes inhibitors. Indian J Microbiol 50:233-7
59. Ramkumar KM, ThayumanaVan B, PalVannan T, Rajaguru P. (2010). Inhibitory effect of Gymnema Montanum leaves on a-glucosidase activity and a-Amylase activity and their relationship with polyphenolic content. Med Chem Res 19:948-61
60. Rawlings ND. (2010). Peptidase inhibitors in the MEROPS database. Biochimie 92:1463-83
61. Roberts RM, Mathialagan N, Duffy JY, Smith GW. (1995). Regulation and regulatory role of proteinase inhibitors. Crit Rev Eukaryot Gene Expr 5:385-436
62. Sakuda S, Isogai A, Matsumoto S, et al. (1986) the structure of allosamidin, a novel insect chitinase inhibitor, produced by Streptomyces sp. Tetrahedron Lett 27:2475-8
63. Sakuda S, Isogai A, Makita T, et al. (1987). Structures of allisamidins, novel insect chitinase inhibitors, produced by Actinomycetes. Agri Biol Chem 51:3251-9
64. Sathiyaseelan K, Stella D. (2012). Isolation and screening of a-glucosidase enzyme inhibitor producing marine actinobacteria isolated from Pichavaram mangrove. Int J Pharm Biol Archive 3: 1142-9
65. Seelmeier S, Schmidt H, Turk V, Von Der Helm K. (1988). Human immunoDeficiency virus has an aspartic-type protease that can be inhibited by pepstatin A. Proc Nat Acad Sci 85: 6612-16
66. Seiberg M, Paine C, Sharlow E, et al. (2000a). Inhibition of melanosome transfer results in skin lightening. J Investigative Dermatol 115:162-7
67. Seiberg M, Paine C, Sharlow E, et al. (2000b) the protease-Activated receptor 2 regulates pigmentation via keratinocyte-melanocyte interactions. Ex Cell Res 254:25-32
68. Skeggs L, Kahn J, Shumway N. (1957) the preparation and function of the angiotensin-converting enzyme. J Ex Med 103:295-9
69. Sorimachi H, Ishiura S, Suzuki K. (1997). Structure and physiological function of calpains. Biochem J 328:721-32
70. Suthindhiran KR, Jayasri M, Kannabiran K. (2009). a-glucosidase and a-Amylase inhibitory activity of Micromonospora sp. VITSDK3 (EU551238). Int J Integrative Biol 6:115-20
71. Takeuchi T, Ogawa K, Iinuma H, et al. (1973). Monoamine oxidase inhibitors isolated from fermented broths. J Antibiot 26: 162-7
72. Tews I, Terwisscha Van Scheltinga AC, Perrakis A, et al. (1997). Substrate-Assisted catalysis unifies two families of chitinolytic enzymes. J Am Chem Soc 119:7954-9
73. Tobey NA, Hosseini SS, Caymaz-Bor C, et al. (2001) the role of pepsin in acid injury to esophageal epithelium. Am J Gastroenterol 96: 3062-70
74. Tokdar P, Ranadive P, Mascarenhas M, et al. (2011). A new pancreatic lipase inhibitor produced by a Streptomyces sp. MTCC 5219. Int Conference Life Sci Technol 3:7-10
75. Tomita K, Oda N, Ohbayashi M, et al. (1990). A new screening method for melanin biosynthesis inhibitors using Streptomyces bikiniensis. J Antibiot 43:1601-5
76. Truscheit E, Frommer W, Junge B, et al. (1981). Chemistry and biochemistry of microbial a-glucosidase inhibitors. Angew Chem Int Ed 20:744-61
77. Tsuru D, Fujiwara K, Kunio K. (1978). Purification and characterization of L-pyrrolidonecarboxylate peptidase from Bacillus amyloliquefaciens. J Biochem 84:467-76
78. Umezawa H. (1972). Enzyme inhibitors of microbial origin. Tokyo, Japan: University of Tokyo Press
79. Umezawa H. (1982). Low-molecular-weight enzyme inhibitors of microbial origin. Ann Rev Microbiol 36:75-99
80. Vernekar JV, Ghatge MS, DeshpanDe VV. (1999). Alkaline protease inhibitor: a novel class of antifungal proteins against phytopathogenic fungi. Biochem Biophy Res Commun 262:702-7
81. Vertesy L, Oeding V, BenDer R, et al. (1984). Tendamistat (HOE 467), a tight-binding a-Amylase inhibitor from Streptomyces tendae 4158. Eur J Biochem 141:505-12
82. Wang L, Hou Y, Peng J, et al. (2012). Bioactivity-based HPLC tanDem Q/TOF for alpha-glucosidase inhibitors. Screening, iDentification, and quantification from Actinomycetes. Lat Am J Pharm 31: 693-8
83. Wehmeier U, Piepersberg W. (2004). Biotechnology and molecular biology of the a-glucosidase inhibitor acarbose. Appl Microbiol Biotechnol 63:613-25
84. Weibel E, Hadvary P, Hochuli E, et al. (1987). Lipstatin, an inhibitor of pancreatic lipase, produced by Streptomyces toxytricini. I. Producing organism, fermentation, isolation and biological activity. J Antibiot 40:1081-5
85. Yamamoto N. (1997). Antihypertensive peptiDes Derived from food proteins. PeptiDe Sci 43:129-34
86. Yamamoto N, Maeno M, Takano T. (1999). Purification and characterization of an antihypertensive peptiDe from a yogurt-like product fermented by Lactobacillus helveticus CPN4. J Dairy Sci 82:1388-93
87. Yoon S-H, Robyt JF. (2003). Study of the inhibition of four alpha amylases by acarbose and its 4IV-A-maltohexaosyl and 4IV-A-maltodoDecaosyl analogues. Carbohyd Res 338:1969-80
88. Zhu Y-P, Yin L-J, Cheng Y-Q, et al. (2008). Effects of sources of carbon and nitrogen on production of a-glucosidase inhibitor by a newly isolated strain of Bacillus subtilis B2. Food Chem 109: 737-42