Applied Biochemistry and Biotechnology

, Volume 186, Issue 1, pp 186–198 | Cite as

Structural Properties of Macrodontain I, a Cysteine Protease from Pseudananas macrodontes (Morr.) Harms (Bromeliaceae)

  • María E. Errasti
  • Claudia L. Natalucci
  • Néstor O. Caffini
  • Alejandra E. Rotelli
  • Adriana Brullo
  • Bruno Maras
  • Sebastián A. Trejo
  • Laura M. I. LópezEmail author


The primary structure of macrodontain I, a peptidase from Pseudananas macrodontes fruits, was determined using Edman’s degradation. The enzyme is a non-glycosylated peptidase composed by 213 amino acids with a calculated molecular weight of 23,486.18 Da, pI value 6.99, and a molar extinction coefficient at 280 nm of 61,685 M−1 cm−1. The alignment of the sequence of macrodontain I with those cysteine peptidases from species belonging to the family Bromeliaceae showed the highest identity degree (87.74%) against fruit bromelain. A remarkable fact is that all these peptidase sequences show two Met contiguous residues (Met121 and 122) and the nonapeptide VPQSIDWRD located in the mature N-terminal region. Residues Cys26 and His159, which constitute the catalytic dyad in all cysteine peptidases, as well as active site residues Gln20 and Asn176, characteristic of Clan C1A, are conserved in macrodontain I. The 3-D model suggests that the enzyme belongs to the α + β class of proteins, with two disulfide bridges (Cys23-Cys63 and Cys57-Cys96) in the α domain, while the β domain is stabilized by another disulfide bridge (Cys153-Cys201). Further, we were able to establish that the cysteine peptidases from P. macrodontes are involved in the anti-inflammatory activity.


Pseudananas macrodontes Bromeliaceae Amino acid sequence Anti-inflammatory activity Cysteine peptidase Plant endopeptidase Macrodontain I 



Cyanogen bromide




High-performance liquid chromatography


Polyvinylidene fluoride


Matrix-assisted laser desorption ionization-time-of-flight mass spectrometry


Reversed phase


Trifluoroacetic acid



M.E. Errasti is a member of the CICPBA Researcher Career. S.A. Trejo and L.M.I. López are members of the CONICET Researcher Career. The present work was supported by grants from CONICET (PIP 297) and CICPBA.

Compliance with Ethical Standards

Conflict of Interest

The authors declare no conflict of interests.

Supplementary material

12010_2018_2725_MOESM1_ESM.doc (30 kb)
Table S1 (DOC 30 kb)
12010_2018_2725_MOESM2_ESM.docx (322 kb)
Table S2 (DOCX 322 kb)


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Copyright information

© Springer Science+Business Media, LLC, part of Springer Nature 2018

Authors and Affiliations

  • María E. Errasti
    • 1
  • Claudia L. Natalucci
    • 2
  • Néstor O. Caffini
    • 2
  • Alejandra E. Rotelli
    • 3
  • Adriana Brullo
    • 4
  • Bruno Maras
    • 4
  • Sebastián A. Trejo
    • 5
  • Laura M. I. López
    • 1
  1. 1.CITEC, INTI-CICPBABuenos AiresArgentina
  2. 2.CIPROVEUNLP- CICPBABuenos AiresArgentina
  3. 3.Laboratory of Pharmacology, Faculty of Chemistry, Biochemistry and PharmacyNational University of San LuisSan LuisArgentina
  4. 4.Dipartimento di Scienze Biochimiche, Facoltà di MedicinaUniversità La SapienzaRomeItaly
  5. 5.Laboratorio de Neurofisiología del Instituto Multidisciplinar de Biología Celular (IMBICE)Buenos AiresArgentina

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