Literature DB >> 5673531

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

S S Husain, G Lowe.   

Abstract

Papain 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 the radioactive peptides were purified chromatographically. Their amino acid composition indicated that cysteine-25 and histidine-106 were cross-linked. Since cysteine-25 is known to be the active-site cysteine residue, histidine-106 must be the active-site histidine residue.

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Year:  1968        PMID： 5673531      PMCID： PMC1198893          DOI： 10.1042/bj1080861

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


  12 in total

1.  ION-EXCHANGE CHROMATOGRAPHY OF AMINO-ACIDS: IMPROVEMENTS IN THE SINGLE COLUMN SYSTEM.

Authors:  A R THOMSON; B J MILES
Journal:  Nature       Date:  1964-08-01       Impact factor: 49.962

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.  The preparation and enzymatic hydrolysis of reduced and S-carboxymethylated proteins.

Authors:  A M CRESTFIELD; S MOORE; W H STEIN
Journal:  J Biol Chem       Date:  1963-02       Impact factor: 5.157

5.  The structure of human hemoglobin. III. The sequence of amino acids in the tryptic peptides of the alpha chain.

Authors:  W KONIGSBERG; R J HILL
Journal:  J Biol Chem       Date:  1962-08       Impact factor: 5.157

6.  Chymotryptic digest of papain.

Authors:  A LIGHT; E L SMITH
Journal:  J Biol Chem       Date:  1962-08       Impact factor: 5.157

7.  Stereospecific alkylation with asymmetric reagents.

Authors:  K Wallenfels; B Eisele
Journal:  Eur J Biochem       Date:  1968-01

8.  Structure of papain.

Authors:  J Drenth; J N Jansonius; R Koekoek; H M Swen; B G Wolthers
Journal:  Nature       Date:  1968-06-08       Impact factor: 49.962

9.  Beta-aspartyl peptide formation from an amino acid sequence in ribonuclease.

Authors:  E E Haley; B J Corcoran
Journal:  Biochemistry       Date:  1967-09       Impact factor: 3.162

10.  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
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  10 in total

1.  Characterization of the papain active centre by using two-protonic-state electrophiles as reactivity probes. Evidence for nucleophilic reactivity in the un-interrupted cysteine-25-histidine-159 interactive system.

Authors:  M Shipton; K Brochlehurst
Journal:  Biochem J       Date:  1978-05-01       Impact factor: 3.857

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

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

3.  A reinvestigation of residues 64-68 and 175 in papain. Evidence that residues 64 and 175 are asparagine.

Authors:  S S Husain; G Lowe
Journal:  Biochem J       Date:  1970-02       Impact factor: 3.857

4.  A general framework of cysteine-proteinase mechanism deduced from studies on enzymes with structurally different analogous catalytic-site residues Asp-158 and -161 (papain and actinidin), Gly-196 (cathepsin B) and Asn-165 (cathepsin H). Kinetic studies up to pH 8 of the hydrolysis of N-alpha-benzyloxycarbonyl-L-arginyl-L-arginine 2-naphthylamide catalysed by cathepsin B and of L-arginine 2-naphthylamide catalysed by cathepsin H.

Authors:  F Willenbrock; K Brocklehurst
Journal:  Biochem J       Date:  1985-04-15       Impact factor: 3.857

5.  Evidence for a two-state transition in papain that may have no close analogue in ficin. Differences in the disposition of cationic sites and hydrophobic binding areas in the active centres of papain and ficin.

Authors:  K Brocklehurst; J P Malthouse
Journal:  Biochem J       Date:  1980-12-01       Impact factor: 3.857

6.  Preparation of fully active ficin from Ficus glabrata by covalent chromatography and characterization of its active centre by using 2,2'-depyridyl disulphide as a reactivity probe.

Authors:  J P Malthouse; K Brocklehurst
Journal:  Biochem J       Date:  1976-11       Impact factor: 3.857

7.  Evidence for histidine in the active sites of ficin and stem-bromelain.

Authors:  S S Husain; G Lowe
Journal:  Biochem J       Date:  1968-11       Impact factor: 3.857

8.  Investigation of the active site of papain with fluorescent probes.

Authors:  G Allen; G Lowe
Journal:  Biochem J       Date:  1973-08       Impact factor: 3.857

9.  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

10.  Cathepsin B, the lysosomal thiol proteinase of calf liver.

Authors:  O Snellman
Journal:  Biochem J       Date:  1969-10       Impact factor: 3.857
  10 in total

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