Thermostable Bacterial Collagenolytic Proteases: A Review

키워드

참고문헌 (94)

1. Cui N, "Biochemical and biological attributes of matrix metalloproteinases", Prog. Mol. Biol. Transl, 147, pp.1~73 (2017)
2. Kadler KE, "Collagens at a glance", J. Cell Sci, 120, pp.1955~1958 (2007)
3. Gordon MK, "Collagens", Cell Tissue Res, 339, pp.247~257 (2010)
4. Ricard-Blum S, "The collagen family", Cold Spring Harbor Perspect. Biol, 3, pp.a004978~ (2011)
5. Shekhter AB, "Collagenolytic enzymes and their applications in biomedicine", Curr. Med. Chem, 26, pp.487~505 (2019)
6. Bella J, "Collagen structure : new tricks from a very old dog", Biochem. J, 473, pp.1001~1025 (2016)
7. Zhang YZ, "Diversity, structures, and collagen-degrading mechanisms of bacterial collagenolytic proteases", Appl. Environ. Microbiol, 81, pp.6098~6107 (2015)
8. Shoulders MD, "Collagen structure and stability", Annu. Rev. Biochem, 78, pp.929~958 (2009)
9. Harrington DJ, "Bacterial collagenases and collagen-degrading enzymes and their potential role in human disease", Infect. Immun, 64, pp.1885~1891 (1996)
10. Bond MD, "Characterization of the individual collagenases from Clostridium histolyticum", Biochemistry, 23, pp.3085~3091 (1984)
11. Matsushita O, "Gene duplication and multiplicity of collagenases in Clostridium histolyticum", J. Bacteriol, 181, pp.923~933 (1999)
12. Duarte AS, "Bacterial collagenases-A review", Crit. Rev. Microbiol, 42, pp.106~126 (2016)
13. Zhang YZ, "Diversity, structures, and collagen-degrading mechanisms of bacterial collagenolytic proteases", Appl. Environ. Microb, 81, pp.6098~6107 (2015)
14. Berti PJ, "Alignment", phylogeny of the papain superfamily of cysteine proteases, 1995, pp.246, 273~283
15. Wilkesman J, "Cysteine protease zymography : Brief review", Methods Mol. Biol, 1626, pp.25~31 (2017)
16. Elleuche S, "Exploration of extremophiles for high temperature biotechnological processes", Curr. Opin. Microbiol, 25, pp.113~119 (2015)
17. Zhang K, "Maturation process and characterization of a novel thermostable and halotolerant subtilisin-like protease with high collagenolytic activity but low gelatinolytic activity", Appl. Environ. Microbiol, 88, pp.e0218421~ (2022)
18. Suzuki Y, "Decomposition of extremely hard-to-degrade animal proteins by thermophilic bacteria", J. Biosci. Bioeng, 102, pp.73~81 (2006)
19. Wang Y, "Mechanistic insight into the fragmentation of type I collagen fibers into peptides and amino acids by a Vibrio collagenase", Appl. Environ. Microbiol, 88, pp.e0167721~ (2022)
20. Huang J, "C-terminal domains of bacterial proteases : structure, function and the biotechnological applications", J. Appl. Microbiol, 122, pp.12~22 (2017)
21. Nonaka T, "The crystal structure of an oxidatively stable subtilisin-like alkaline serine protease, KP-43, with a C-terminal β-barrel domain", J. Biol. Chem, 279, pp.47344~47351 (2004)
22. Philominathan ST, "Unidirectional binding of clostridial collagenase to triple helical substrates", J. Biol. Chem, 284, pp.10868~10876 (2009)
23. Ohbayashi N, "Enhancement of the structural stability of fulllength clostridial collagenase by calcium ions", Appl. Environ. Microbiol, 78, pp.5839~5844 (2012)
24. Eckhard U, "Structural basis for activity regulation and substrate preference of clostridial collagenases G, H, and T", J. Biol. Chem, 288, pp.20184~20194 (2013)
25. Takeuchi H, "Structural gene and complete amino acid sequence of Vibrio alginolyticus collagenase", Biochem. J, 281, pp.703~708 (1992)
26. Kim SK, "Cloning and sequence analysis of a novel metalloprotease gene from Vibrio parahaemolyticus 04", Gene, 283, pp.277~286 (2002)
27. Lee JH, "The FAXWXXT motif in the carboxyl terminus of Vibrio mimicus metalloprotease is involved in binding to collagen", FEBS Lett, 579, pp.2507~2513 (2005)
28. Punta M, "The Pfam protein families database", Nucleic Acids Res, 40, pp.D290~D301 (2012)
29. Rawlings ND, "MEROPS : the peptidase database", Nucleic Acids Res, 38, pp.D227~D233 (2010)
30. Matsushita O, "Purification and characterization of Clostridium perfringens 120-kilodalton collagenase and nucleotide sequence of the corresponding gene", J. Bacteriol, 176, pp.149~156 (1994)
31. Bruggemann H, "The genome sequence of Clostridium tetani, the causative agent of tetanus disease", Proc. Natl. Acad. Sci. USA, 100, pp.1316~1321 (2003)
32. Donahue TR, "Collagenase and surgical disease", Hernia, 10, pp.478~485 (2006)
33. Eckhard U, "Structure of collagenase G reveals a chew-and-digest mechanism of bacterial collagenolysis", Nat. Struct. Mol. Biol, 18, pp.1109~1114 (2011)
34. Maclennan JD, "Bacterial digestion of collagen", J. Clin. Invest, 32, pp.1317~1322 (1953)
35. Breite AG, "Characterization and functional assessment of Clostridium histolyticum class I(C1)collagenases and the synergistic degradation of native collagen in enzyme mixtures containing class II(C2)collagenase", Transplant. Proc, 43, pp.3171~3175 (2011)
36. French MF, "Limited proteolysis of type I collagen at hyperreactive sites by class I and II Clostridium histolyticum collagenases : complementary digestion patterns", Biochemistry, 26, pp.681~687 (1987)
37. Lee CY, "Molecular analysis of an extracellular protease gene from Vibrio parahaemolyticus", Microbiology(Reading, England), 141, pp.2569~2576 (1995)
38. Lee JH, "Isolation and sequence analysis of metalloprotease gene from Vibrio mimicus", Biochim. Biophys. Acta, 1384, pp.1~6 (1998)
39. Luan X, "Expression and characterization of a metalloprotease from a Vibrio parahaemolyticus isolate", Can. J. Microbiol, 53, pp.1168~1173 (2007)
40. French MF, "Identification of Clostridium histolyticum collagenase hyperreactive sites in type I, II, and III collagens : lack of correlation with local triple helical stability", J. Protein Chem, 11, pp.83~97 (1992)
41. Lecroisey A, "Differences in the degradation of native collagen by two microbial collagenases", Biochem. J, 179, pp.53~58 (1979)
42. Ueshima S, "Insights into the catalytic mechanism of collagenase through structural and mutational analyses", FEBS Lett, 597, pp.2473~2483 (2023)
43. Wang Y, "Structure of collagenase VhaC provides insight into the mechanism of bacterial collagenolysis", Nat. Commun, 13, pp.566~ (2022)
44. Hoa Bach TM, "Characterization of collagenase found in the nonpathogenic bacterium Lysinibacillus sphaericus VN3", Biosci. Biotechnol. Biochem, 84, pp.2293~2302 (2020)
45. Ramírez-Rico G, "Identification, biochemical characterization, and in vivo detection of a Zn-metalloprotease with collagenase activity from A2", Int. J. Mol. Sci, 25, pp.1289~ (2024)
46. Uesugi Y, "Two bacterial collagenolytic serine proteases have different topological specificities", Bba-Proteins Proteom, 1784, pp.716~726 (2008)
47. Wlodawer A, "Structural and enzymatic properties of the sedolisin family of serine-carboxyl peptidases", Acta Biochim. Polonica, 50, pp.81~102 (2003)
48. Rawlings ND, "MEROPS : the peptidase database", Nucleic Acids Res, 38, pp.D227~D233 (2010)
49. Wlodawer A, "Structural and enzymatic properties of the sedolisin family of serine-carboxyl peptidases", Acta Biochim. Pol, 50, pp.81~102 (2003)
50. Rawlings ND, "Handbook of proteolytic enzymes", pp.2491~2505 (2013), Elsevier
51. Nakayama T, "Thermostable collagenolytic activity of a novel thermophilic isolate, Bacillus sp. strain NTAP-1", J. Biosci. Bioeng, 89, pp.612~614 (2000)
52. Tsuruoka N, "Alicyclobacillus sendaiensis sp. nov., a novel acidophilic, slightly thermophilic species isolated from soil in Sendai, Japan", Int. J. Syst. Evol. Microbiol, 53, pp.1081~1084 (2003)
53. Tsuruoka N, "Collagenolytic serine-carboxyl proteinase from Alicyclobacillus sendaiensis strain NTAP-1 : purification, characterization, gene cloning, and heterologous expression", Appl. Environ. Microbiol, 69, pp.162~169 (2003)
54. Nakayama T, "Thermostable collagenolytic activity of a novel thermophilic isolate, Bacillus sp. strain NTAP-1", J. Biosci. Bioeng, 89, pp.612~614 (2000)
55. Wlodawer A, "Crystallographic and biochemical investigations of kumamolisin-As, a serine-carboxyl peptidase with collagenase activity", J. Biol. Chem, 279, pp.21500~21510 (2004)
56. Leikina E, "Type I collagen is thermally unstable at body temperature", Proc. Natl. Acad. Sci. USA, 99, pp.1314~1318 (2002)
57. Catara G, "A new kumamolisin-like protease from : : an enzyme active under extreme acidic conditions", Biocatal. Biotransfor, 24, pp.358~370 (2006)
58. Okamoto M, "A thermostable collagenolytic protease with a very large molecular mass produced by thermophilic Bacillus sp. strain MO-1", Appl. Microbiol. Biotechnol, 57, pp.103~108 (2001)
59. Itoi Y, "Characteristic features in the structure and collagen-binding ability of a thermophilic collagenolytic protease from the thermophile Geobacillus collagenovorans MO-1", J. Bacteriol, 188, pp.6572~6579 (2006)
60. Kurata A, "Collagenolytic subtilisin-like protease from the deep-sea bacterium Alkalimonas collagenimarina AC40T", Appl. Microbiol. Biotechnol, 86, pp.589~598 (2010)
61. Petrova DH, "Novel thermostable serine collagenase from Thermoactinomyces sp. 21E: purification and some properties", J. Basic Microbiol, 46, pp.275~285 (2006)
62. Zhao GY, "Hydrolysis of insoluble collagen by deseasin MCP-01 from deepsea Pseudoalteromonas sp. SM9913: collagenolytic characters, collagen-binding ability of C-terminal polycystic kidney disease domain, and implication for its novel role in deep-sea sedimentary particulate organic nitrogen degradation", J. Biol. Chem, 283, pp.36100~36107 (2008)
63. Wang YK, "Mechanistic insight into the function of the C-terminal PKD domain of the collagenolytic serine protease deseasin MCP-01 from deep sea Pseudoalteromonas sp. SM9913: binding of the PKD domain to collagen results in collagen swelling but does not unwind the collagen triple helix", J. Biol. Chem, 285, pp.14285~14291 (2010)
64. Ran LY, "Structural and mechanistic insights into collagen degradation by a bacterial collagenolytic serine protease in the subtilisin family", Mol. Microbiol, 90, pp.997~1010 (2013)
65. Ran LY, "Characterization of a novel subtilisin-like protease myroicolsin from deep sea bacterium Myroides profundi D25 and molecular insight into its collagenolytic mechanism", J. Biol. Chem, 289, pp.6041~6053 (2014)
66. Chen XL, "A novel type of subtilase from the psychrotolerant bacterium Pseudoalteromonas sp. SM9913: catalytic and structural properties of deseasin MCP-01", Microbiology (Reading), 153, pp.2116~2125 (2007)
67. Zhao GY, "Hydrolysis of insoluble collagen by deseasin MCP-01 from deepsea Pseudoalteromonas sp. SM9913: collagenolytic characters, collagen-binding ability of C-terminal polycystic kidney disease domain, and implication for its novel role in deep-sea sedimentary particulate organic nitrogen degradation", J. Biol. Chem, 283, pp.36100~36107 (2008)
68. Ran LY, "Structural and mechanistic insights into collagen degradation by a bacterial collagenolytic serine protease in the subtilisin family", Mol. Microbiol, 90, pp.997~1010 (2013)
69. Muhammed NS, "Recombinant production and characterization of an extracellular subtilisin-like serine protease from of fermented food origin", Protein J, 40, pp.419~435 (2021)
70. Ding YD, "Extracellular production, characterization, and engineering of a polyextremotolerant subtilisin-like protease from feather-degrading strain CDF", Front. Microbiol, 11, pp.605771~ (2020)
71. Huang J, "Mechanistic insight into the binding and swelling functions of prepeptidase C-terminal(PPC)domains from various bacterial proteases", Appl. Environ. Microbiol, 85, pp.e00611-19~ (2019)
72. Leikina E, "Type I collagen is thermally unstable at body temperature", Proc. Natl. Acad. Sci. USA, 99, pp.1314~1318 (2002)
73. Foophow T, "Crystal structure of a subtilisin homologue, Tk-SP, from Thermococcus kodakaraensis : requirement of a C-terminal beta-jelly roll domain for hyperstability", J. Mol. Biol, 400, pp.865~877 (2010)
74. Shekhter AB, "Collagenolytic enzymes and their applications in biomedicine", Curr. Med. Chem, 26, pp.487~505 (2019)
75. Myers LK, "Characterization of a peptide analog of a determinant of type II collagen that suppresses collagen-induced arthritis", J. Immunol, 161, pp.3589~3595 (1998)
76. Aumiller WM Jr., "Coupled enzyme reactions performed in heterogeneous reaction media: experiments and modeling for glucose oxidase and horseradish peroxidase in a PEG", citrate aqueous two-phase system, 2014, pp.118, 2506~2517
77. Ku G, "Prevention of experimental autoimmune arthritis with a peptide fragment of type II collagen", Eur. J. Immunol, 23, pp.591~599 (1993)
78. Miller EJ, "The collagens : an overview and update", Methods Enzymol, 144, pp.3~41 (1987)
79. Watanabe K, "Collagenolytic proteases from bacteria", Appl. Microbiol. Biotechnol, 63, pp.520~526 (2004)
80. Nitulescu G, "Discovery of new microbial collagenase inhibitors", Life, 12, pp.2114~ (2022)
81. Rajabimashhadi Z, "Collagen derived from fish industry waste : Progresses and challenges", Polymers(Basel), 15, pp.344~ (2023)
82. Okamoto M, "A thermostable collagenolytic protease with a very large molecular mass produced by Thermophilic sp. strain MO-1", Appl. Microbiol. Biotechnol, 57, pp.103~108 (2001)
83. Kurata A, "Collagenolytic subtilisin-like protease from the deep-sea bacterium Alkalimonas collagenimarina AC40", Appl. Microbiol. Biotechnol, 86, pp.589~598 (2010)
84. Petrova DH, "Novel thermostable serine collagenase from sp 21E : : purification and some properties", J. Basic Microb, 46, pp.275~285 (2006)
85. Bai Y, "Extremely acidic beta-1,4-glucanase, CelA4, from thermoacidophilic Alicyclobacillus sp. A4 with high protease resistance and potential as a pig feed additive", J. Agric. Food Chem, 58, pp.1970~1975 (2010)
86. Eckhard U, "Biochemical characterization of the catalytic domains of three different clostridial collagenases", Biol. Chem, 390, pp.11~18 (2009)
87. Santra M, "Studies on Vibrio mimicus derived collagenase variants providing insights into critical role(s)played by the FAXWXXT motifs in its collagen-binding domain", Enzyme Microb. Technol, 147, pp.109779~ (2021)
88. Lee JH, "Characterization of the enzyme activity of an extracellular metalloprotease(VMC)from Vibrio mimicus and its C-terminal deletions", FEMS Microbiol. Lett, 223, pp.293~300 (2003)
89. Tanaka K, "Recombinant collagenase from Grimontia hollisae as a tissue dissociation enzyme for isolating primary cells", Sci. Rep, 10, pp.3927~ (2020)
90. Bhuimbar MV, "Purification, characterization and application of collagenolytic protease from Bacillus subtilis strain MPK", J. Biosci. Bioeng, 38, pp.21~28 (2024)
91. Serwanja J, "A conserved strategy to attack collagen : The activator domain in bacterial collagenases unwinds triple-helical collagen", Proc. Natl. Acad. Sci. USA, 121, pp.e2321002121~ (2024)
92. Li HJ, "Characterization of a new S8 serine protease from marine sedimentary Photobacterium sp. A5-7 and the function of its protease-associated domain", Front. Microbiol, 7 (2016)
93. Itoi Y, "Characteristic features in the structure and collagen-binding ability of a thermophilic collagenolytic protease from the thermophile MO-1", J. Bacteriol, 188, pp.6572~6579 (2006)
94. Teramura N, "Cloning of a novel collagenase gene from the gramnegative bacterium Grimontia(Vibrio)hollisae 1706B and its efficient expression in Brevibacillus choshinensis", J. Bacteriol, 193, pp.3049~3056 (2011)

관련 논문AI추천