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Literature DB >> 5420046

The amino acid sequence around the active-site cysteine and histidine residues of stem bromelain.

Abstract

Stem bromelain that had been irreversibly inhibited with 1,3-dibromo[2-(14)C]-acetone was reduced with sodium borohydride and carboxymethylated with iodoacetic acid. After digestion with trypsin and alpha-chymotrypsin three radioactive peptides were isolated chromatographically. The amino acid sequences around the cross-linked cysteine and histidine residues were determined and showed a high degree of homology with those around the active-site cysteine and histidine residues of papain and ficin.

Entities: Chemical

Mesh：

Substances：

Year: 1970 PMID： 5420046 PMCID： PMC1178867 DOI： 10.1042/bj1170341

Source DB: PubMed Journal: Biochem J ISSN： 0264-6021 Impact factor: 3.857

7 in total

1. PREPARATION AND CHEMICAL PROPERTIES OF PURIFIED STEM AND FRUIT BROMELAINS.

Authors: S OTA; S MOORE; W H STEIN
Journal: Biochemistry Date: 1964-02 Impact factor: 3.162

2. CHROMATOGRAPHY OF PEPSIN AND CHYMOTRYPSIN DIGESTS OF EGG WHITE LYSOZYME ON PHOSPHOCELLULOSE.

Authors: R E CANFIELD; C B ANFINSEN
Journal: J Biol Chem Date: 1963-08 Impact factor: 5.157

3. CURRENT STATUS OF THE STRUCTURE OF PAPAIN: THE LINEAR SEQUENCE, ACTIVE SULFHYDRYL GROUP, AND THE DISULFIDE BRIDGES.

Authors: A LIGHT; R FRATER; J R KIMMEL; E L SMITH
Journal: Proc Natl Acad Sci U S A Date: 1964-11 Impact factor: 11.205

4. Sequence of amino acids in the vicinity of the reactive thiol group of stem bromelain.

Authors: L P Chao; I E Liener
Journal: Biochem Biophys Res Commun Date: 1967-04-07 Impact factor: 3.575

5. The location of the active-site histidine residue in the primary sequence of papain.

Authors: S S Husain; G Lowe
Journal: Biochem J Date: 1968-08 Impact factor: 3.857

6. The amino acid sequence around the active-site cysteine and histidine residues, and the buried cysteine residue in ficin.

Authors: S S Husain; G Lowe
Journal: Biochem J Date: 1970-04 Impact factor: 3.857

7. Evidence for histidine in the active site of papain.

Authors: S S Husain; G Lowe
Journal: Biochem J Date: 1968-08 Impact factor: 3.857

7 in total

8 in total

1. Kinetic specificity in papain-catalysed hydrolyses.

Authors: G Lowe; Y Yuthavong
Journal: Biochem J Date: 1971-08 Impact factor: 3.857

2. The amino acid sequence of the tryptic peptides from actinidin, a proteolytic enzyme from the fruit of Actinidia chinensis.

Authors: A Carne; C H Moore
Journal: Biochem J Date: 1978-07-01 Impact factor: 3.857

3. 4-Chloro-7-nitrobenzo-2-oxa-1,3-diazole as a reactivity probe for the investigation of the thiol proteinases. evidence that ficin and bromelain may lack carboxyl groups conformationally equivalent to that of aspartic acid-158 of papain.

Authors: M Shipton; T Stuchbury; K Brocklehurst
Journal: Biochem J Date: 1976-11 Impact factor: 3.857

8. Trimethylamine-N-oxide switches from stabilizing nature: A mechanistic outlook through experimental techniques and molecular dynamics simulation.

Authors: Anjeeta Rani; Abhilash Jayaraj; B Jayaram; Venkatesu Pannuru
Journal: Sci Rep Date: 2016-03-30 Impact factor: 4.379