Literature for peptidase S01.280: lysyl endopeptidase (bacteria)

Summary Alignment Tree Sequences Sequence features Distribution Structure Literature Substrates

(Topics flags: S Structure, I Inhibitor, P Specificity, E Expression, V Review. To select only the references relevant to a single topic, click the link above. See explanation.)

    2025
  1. Pourani,Z., Keramati,M., Komijani,S., Golkar,M., Cohan,R.A., Mohseni,N. and Valizadeh,V.
    Efficient periplasmic expression of active lysyl endopeptidase and optimizing the purification methods
    Protein Expr Purif226, 106618-106618. PubMed  Europe PubMed DOI
  2. 2019
  3. Hakobyan,A., Schneider,M.B., Liesack,W. and Glatter,T.
    Efficient tandem LysC/trypsin digestion in detergent conditions
    Proteomicse1900136-e1900136. PubMed  Europe PubMed DOI
  4. 2018
  5. Wu,Z., Huang,J., Huang,J., Li,Q. and Zhang,X.
    Lys-C/Arg-C, a more specific and efficient digestion approach for proteomics studies
    Anal Chem90, 9700-9707. PubMed  Europe PubMed DOI
  6. 2017
  7. Li,Q., Feng,Y., Tan,M.-J. and Zhai,L.-H.
    Evaluation of endoproteinase Lys-C/trypsin sequential digestion used in proteomics sample preparation
    Fenxi Huaxue Chin J Anal Chem45, 316-321. DOI
  8. Takami,H., Toyoda,A., Uchiyama,I., Itoh,T., Takaki,Y., Arai,W., Nishi,S., Kawai,M., Shin-Ya,K. and Ikeda,H.
    Complete genome sequence and expression profile of the commercial lytic enzyme producer Lysobacter enzymogenes M497-1
    DNA Res24, 169-177. PubMed  Europe PubMed DOI
  9. 2016
  10. Giansanti,P., Tsiatsiani,L., Low,T.Y. and Heck,A.J.
    Six alternative proteases for mass spectrometry-based proteomics beyond trypsin
    Nat Protoc11, 993-1006. PubMed  Europe PubMed DOI
  11. Stressler,T., Eisele,T., Meyer,S., Wangler,J., Hug,T., Lutz-Wahl,S. and Fischer,L.
    Heterologous expression and pro-peptide supported refolding of the high specific endopeptidase Lys-C
    Protein Expr Purif118, 31-38. PubMed  Europe PubMed DOI  E
  12. 2015
  13. Tsfasman,I.M., Lapteva,Y.S., Krasovskaya,L.A., Kudryakova,I.V., Vasilyeva,N.V., Granovsky,I.E. and Stepnaya,O.A.
    Gene expression of lytic endopeptidases AlpA and AlpB from Lysobacter sp. XL1 in pseudomonads
    J Mol Microbiol Biotechnol25, 244-252. PubMed  Europe PubMed DOI  E
  14. 2014
  15. Asztalos,P., Muller,A., Holke,W., Sobek,H. and Rudolph,M.G.
    Atomic resolution structure of a lysine-specific endoproteinase from Lysobacter enzymogenes suggests a hydroxyl group bound to the oxyanion hole
    Acta Crystallogr D Biol Crystallogr70, 1832-1843. PubMed  Europe PubMed DOI  S
  16. Gershon,P.D.
    Cleaved and missed sites for trypsin, Lys-C, and Lys-N can be predicted with high confidence on the basis of sequence context
    J Proteome Res13, 702-709. PubMed  Europe PubMed DOI  P
  17. Gokcen,A., Vilcinskas,A. and Wiesner,J.
    Biofilm-degrading enzymes from Lysobacter gummosus
    Virulence5, 378-387. PubMed  Europe PubMed DOI
  18. Kessler,E. and Safrin,M.
    Elastinolytic and proteolytic enzymes
    Methods Mol Biol1149, 135-169. PubMed  Europe PubMed DOI  V
  19. 2013
  20. Achour,B. and Barber,J.
    The activities of Achromobacter lysyl endopeptidase and Lysobacter lysyl endoproteinase as digestive enzymes for quantitative proteomics
    Rapid Commun Mass Spectrom27, 1669-1672. PubMed  Europe PubMed DOI
  21. Ohnishi,Y., Yamada,T., Kurihara,K., Tanaka,I., Sakiyama,F., Masaki,T. and Niimura,N.
    Neutron and X-ray crystallographic analysis of Achromobacter protease I at pD 8.0: Protonation states and hydration structure in the free-form
    Biochim Biophys Acta1834, 1642-1647. PubMed  Europe PubMed DOI  S
  22. 2012
  23. Sakiyama,F. and Masaki,T.
    Lysyl endopeptidase
    [ISSN:978-0-12-407742-3]3, 2543-2545. DOI
  24. 2011
  25. Kishimoto,T., Kondo,J., Takai-Igarashi,T. and Tanaka,H.
    Accurate mass comparison coupled with two endopeptidases enables identification of protein termini
    Proteomics11, 485-489. PubMed  Europe PubMed DOI
  26. 2010
  27. Andersen,A.S., Palmqvist,E., Bang,S., Shaw,A.C., Hubalek,F., Ribel,U. and Hoeg-Jensen,T.
    Backbone cyclic insulin
    J Pept Sci16, 473-479. PubMed  Europe PubMed DOI
  28. Ito,L., Shiraki,K., Uchida,T., Okumura,M. and Yamaguchi,H.
    Crystallization and preliminary crystallographic analysis of Achromobacter protease I mutants
    Acta Crystallograph Sect F Struct Biol Cryst Commun66, 1531-1532. PubMed  Europe PubMed DOI
  29. Kim,J., Jones,L., Taylor,L., Kannan,G., Jackson,F., Lau,H., Latypov,R.F. and Bailey,B.
    Characterization of a unique IgG1 mAb CEX profile by limited Lys-C proteolysis/CEX separation coupled with mass spectrometry and structural analysis
    J Chromatogr B Analyt Technol Biomed Life Sci878, 1973-1981. PubMed  Europe PubMed DOI
  30. Ohnishi,Y., Masaki,T., Yamada,T., Kurihara,K., Tanaka,I. and Niimura,N.
    A preliminary neutron diffraction analysis of Achromobacter protease I
    J Phys Conf Ser251, 012032-012032. DOI  S
  31. Raijmakers,R., Neerincx,P., Mohammed,S. and Heck,A.J.
    Cleavage specificities of the brother and sister proteases Lys-C and Lys-N
    Chem Commun (Camb)46, 8827-8829. PubMed  Europe PubMed DOI  P
  32. 2004
  33. Chohnan,S., Shiraki,K., Yokota,K., Ohshima,M., Kuroiwa,N., Ahmed,K., Masaki,T. and Sakiyama,F.
    A second lysine-specific serine protease from Lysobacter sp. strain IB-9374
    J Bacteriol186, 5093-5100. PubMed  Europe PubMed DOI
  34. Sakiyama,F.
    Lysyl endopeptidase
    [ISSN:0-12-079610-4]2, 1454-1455.  V
  35. 2002
  36. [YEAR:16-7-2002]Chohnan,S., Nonaka,J., Teramoto,K., Taniguchi,K., Kameda,Y., Tamura,H., Kurusu,Y., Norioka,S., Masaki,T. and Sakiyama,F.
    Lysobacter strain with high lysyl endopeptidase production
    FEMS Microbiol Lett213, 13-20. PubMed  Europe PubMed DOI
  37. Shiraki,K. and Sakiyama,F.
    Histidine 210 mutant of a trypsin-type Achromobacter protease I shows broad optimum pH range
    J Biosci Bioeng93, 331-333. PubMed  Europe PubMed
  38. Shiraki,K., Norioka,S., Li,S. and Sakiyama,F.
    Contribution of an imidazole-indole stack to high catalytic potency of a lysine-specific serine protease, Achromobacter protease I
    J Biochem131, 213-218. PubMed  Europe PubMed
  39. Shiraki,K., Norioka,S., Li,S., Yokota,K. and Sakiyama,F.
    Electrostatic role of aromatic ring stacking in the pH-sensitive modulation of a chymotrypsin-type serine protease, Achromobacter protease I
    Eur J Biochem269, 4152-4158. PubMed  Europe PubMed DOI
  40. 1999
  41. Ikai,A., Ookata,K., Shimizu,M., Nakamichi,N., Ito,M. and Matsumura,T.
    A recombinant bait region mutant of human alpha2-macroglobulin exhibiting an altered proteinase-inhibiting spectrum
    Cytotechnology31, 53-60. PubMed  Europe PubMed DOI
  42. 1997
  43. Eriksen,J. and Holm,K.A.
    Automated colorimetric determination of Achromobacter lyticus protease activity in fermentation samples using Tos-Gly-Pro-Lys-pNA as a chromogenic substrate
    Analyst122, 169-172. DOI
  44. 1996
  45. Oda,Y., Kitagawa,Y., Yamaguchi,H., Matsuura,Y., Katsube,Y., Masaki,T., Tanaka,T., Matsuura,S., Norioka,S. and Sakiyama,F.
    Crystallization and preliminary X-ray diffraction analysis of two lysinal derivatives of Achromobacter protease I
    Acta Crystallogr D Biol Crystallogr52, 1027-1029. PubMed  Europe PubMed DOI  I
  46. 1994
  47. Masaki,T., Takiya,T., Kuwahara,S., Soejima,M., Tsunasawa,S. and Sakiyama,F.
    Hydrolysis of S-2-aminoethylcysteinyl peptide bond by Achromobacter protease I
    Biosci Biotechnol Biochem58, 215-216. PubMed  Europe PubMed DOI
  48. [YEAR:24-6-1994]Norioka,S., Ohta,S., Ohara,T., Lim,S.I. and Sakiyama,F.
    Identification of three catalytic triad constituents and Asp-225 essential for function of lysine-specific serine protease, Achromobacter protease I
    J Biol Chem269, 17025-17029. PubMed  Europe PubMed
  49. Sakiyama,F. and Masaki,T.
    Lysyl endopeptidase of Achromobacter lyticus
    Methods Enzymol244, 126-137. PubMed  Europe PubMed DOI  V
  50. 1992
  51. Masaki,T., Tanaka,T., Tsunasawa,S., Sakiyama,F. and Soejima,M.
    Inhibition of Achromobacter protease I by lysinal derivatives
    Biosci Biotechnol Biochem56, 1604-1607. PubMed  Europe PubMed DOI  I
  52. Norioka,S. and Sakiyama,F.
    Lysine-specific serine protease from Achromobacter lyticus: its substrate specificity and comparison with trypsin
    J Protein Chem11, 369-370. DOI
  53. 1989
  54. Ohara,T., Makino,K., Shinagawa,H., Nakata,A., Norioka,S. and Sakiyama,F.
    Cloning, nucleotide sequence, and expression of Achromobacter protease I gene
    J Biol Chem264, 20625-20631. PubMed  Europe PubMed
  55. Tsunasawa,S., Masaki,T., Hirose,M., Soejima,M. and Sakiyama,F.
    The primary structure and structural characteristics of Achromobacter lyticus protease I, a lysine-specific serine protease
    J Biol Chem264, 3832-3839. PubMed  Europe PubMed
  56. 1988
  57. Bank,R.A., Crusius,B.C., Zwiers,T., Meuwissen,S.G., Arwert,F. and Pronk,J.C.
    Identification of a Glu > Lys substitution in the activation segment of human pepsinogen A-3 and -5 isozymogens by peptide mapping using endoproteinase Lys-C
    FEBS Lett238, 105-108. PubMed  Europe PubMed
  58. Van Leuven,F., Marynen,P., Cassiman,J.J. and Van Den Berghe,H.
    Proteolysis of human alpha2-macroglobulin without hydrolysis of the internal thiolesters or expression of the receptor recognition site
    J Biol Chem263, 468-471. PubMed  Europe PubMed
  59. 1986
  60. Van Leuven,F., Marynen,P., Sottrup-Jensen,L., Cassiman,J.J. and Van Den Berghe,H.
    The receptor-binding domain of human alpha2-macroglobulin. Isolation after limited proteolysis with a bacterial proteinase
    J Biol Chem261, 11369-11373. PubMed  Europe PubMed
  61. 1983
  62. Jekel,P.A., Weijer,W.J. and Beintema,J.J.
    Use of endoproteinase Lys-C from Lysobacter enzymogenes in protein sequence analysis
    Anal Biochem134, 347-354. PubMed  Europe PubMed
  63. 1981
  64. Masaki,T., Fujihashi,T., Nakamura,K. and Soejima,M.
    Studies on a new proteolytic enzyme from Achromobacter lyticus M497-1. II. Specificity and inhibition studies of Achromobacter protease I
    Biochim Biophys Acta660, 51-55. PubMed  Europe PubMed
  65. Masaki,T., Tanabe,M., Nakamura,K. and Soejima,M.
    Studies on a new proteolytic enzyme from Achromobacter lyticus M497-1. I. Purification and some enzymatic properties
    Biochim Biophys Acta660, 44-50. PubMed  Europe PubMed
  66. 1978
  67. Masaki,T., Nakamura,K., Isono,M. and Soejima,M.
    A new proteolytic enzyme from Achromobacter lyticus M497-I
    Agric Biol Chem42, 1443-1445.