Bromelain amino acid sequence

A. Ritonja, A. D. Rowan, D. J. Buttle, N. D. Rawlings, V. Turk, and A. J. Barrett. Stem bromelain amino acid sequence and implications for weak binding of cystatin. FEBS Lett. 247 419 (1989). 

G, Kamphuis, J. Drentii, and E. N. Baker. Thiol protease. Comparative studies based on the high-resolution structures of papain and actinidin, and an amino acid sequence information far cathenaim B and R and stem bromelain. J. MoL BioL /62 317 (19B5). 

Figure 1 Alignment of the amino acid sequences of stem bromelain and papain. Amino adds identical for both sequences are boxed. Bioin Anaco Bromelain from Ananas comasun Papa Carpa papain from Cariea papaya. (Sequences were extracted from the SwissProt protean sequence dara base.)...

His1 0 and orients it for its catalytic function [54], The putative catalytic thiolate-imldazollum pair at the active site of bromelain is thus, by comparison of the amino acid sequence of bromelain with other cysteine protein ases, likely to have a different conformation from that in (he cysteine proteinases (hat aie tightly inhibited by cystatin [45]. Bromelain also distinguishes itself from other cysteine protein ases by its slow inhibition by the irreversible inhibitor of cysteine oroteinases E-64 rW-ft 3-fraw-cari)OKVOxiran-2 BrboiwlVL-leucvn-amido 4-... 

Ritonja et al. [45] revealed the complete amino acid sequence of stem bromelain. Their results show that stem bromelain exists as a single polypeptide chain with... 

S. S. Hussain and G. Lowe. The amino acid sequence around the active-site cysteine and histidine residues of stem bromelain. Biochem. J. 7/7 341 (1970). 

A family of cysteine proteinase inhibitors different from the cystatin super-family was Isolated from pineapple stem acetone powder. These inhibitors have a Mr of about 5800 and are composed of a longer (41 amino acids) and a shorter (1L ammo acids) peptide chain connected with disulfide bonds [29]. The conserved sequence Gin- fal-Val-AJa-Gly of the cystatins is not present in these inhibitors, indicating a different mechanism of interaction. The bromelain inhibitor VI was found to share similar folding and disulfide band connectivities with the Bowman-Bilk trypsiu/chymatrypsm inhibitor from soybean [30,31]. Hie physiological role of these inhibitors remains undear. 

Stem bromelain is able to interact with two or more sequential amino acids in a peptide substrate, demonstrated by using N-benzyloxycarbonyl-L-phenylalanyl-L-serine methyl ester [36]. A glutamic acid residue in position P3 prevents cleavage of the susceptible peptide bond. The sequences containing negatively charged residues in position P3 and P4 remain intact [37]. 

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