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

Abstract:

: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.

authors

Errasti ME,Natalucci CL,Caffini NO,Rotelli AE,Brullo A,Maras B,Trejo SA,López LMI

doi

10.1007/s12010-018-2725-3

subject

Has Abstract

pub_date

2018-09-01 00:00:00

pages

186-198

issue

1

eissn

0273-2289

issn

1559-0291

pii

10.1007/s12010-018-2725-3

journal_volume

186

pub_type

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