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1
Evidence for histidine in the active site of papain.
Biochem J. 1968 Aug;108(5):855-9. doi: 10.1042/bj1080855.
2
Evidence for histidine in the active sites of ficin and stem-bromelain.
Biochem J. 1968 Nov;110(1):53-7. doi: 10.1042/bj1100053.
3
The location of the active-site histidine residue in the primary sequence of papain.
Biochem J. 1968 Aug;108(5):861-6. doi: 10.1042/bj1080861.
4
Reaction of papain with -bromo- -(5-imidazolyl)propionic acid.
Biochemistry. 1972 Jan 18;11(2):164-9. doi: 10.1021/bi00752a005.
5
A reinvestigation of residues 64-68 and 175 in papain. Evidence that residues 64 and 175 are asparagine.
Biochem J. 1970 Feb;116(4):689-92. doi: 10.1042/bj1160689.
6
The activation of papain and the inhibition of the active enzyme by carbonyl reagents.
J Biol Chem. 1969 Nov 10;244(21):5928-35.
7
Reaction of glyceraldehyde-3-phosphate dehydrogenase with dibromoacetone.
Biochemistry. 1972 Sep 26;11(20):3753-62. doi: 10.1021/bi00770a013.
8
The amino acid sequence around the active-site cysteine and histidine residues, and the buried cysteine residue in ficin.
Biochem J. 1970 Apr;117(2):333-40. doi: 10.1042/bj1170333.
9
Selective cysteine modification in glyceraldehyde-3-phosphate dehydrogenase.
Biochemistry. 1972 Sep 26;11(20):3762-70. doi: 10.1021/bi00770a014.
10
The amino acid sequence around the active-site cysteine and histidine residues of stem bromelain.
Biochem J. 1970 Apr;117(2):341-6. doi: 10.1042/bj1170341.
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Targeting the SARS-CoV-2 main protease using FDA-approved Isavuconazonium, a P2-P3 α-ketoamide derivative and Pentagastrin: An in-silico drug discovery approach.
J Mol Graph Model. 2020 Dec;101:107730. doi: 10.1016/j.jmgm.2020.107730. Epub 2020 Sep 2.
2
Structural basis of substrate recognition by a polypeptide processing and secretion transporter.
Elife. 2020 Jan 14;9:e51492. doi: 10.7554/eLife.51492.
3
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.
Biochem J. 1980 Dec 1;191(3):707-18. doi: 10.1042/bj1910707.
4
Current problems in mechanistic studies of serine and cysteine proteinases.
Biochem J. 1982 Oct 1;207(1):1-10. doi: 10.1042/bj2070001.
5
Evidence for histidine in the active sites of ficin and stem-bromelain.
Biochem J. 1968 Nov;110(1):53-7. doi: 10.1042/bj1100053.
6
The location of the active-site histidine residue in the primary sequence of papain.
Biochem J. 1968 Aug;108(5):861-6. doi: 10.1042/bj1080861.
7
A reinvestigation of residues 64-68 and 175 in papain. Evidence that residues 64 and 175 are asparagine.
Biochem J. 1970 Feb;116(4):689-92. doi: 10.1042/bj1160689.
8
The amino acid sequence around the active-site cysteine and histidine residues of stem bromelain.
Biochem J. 1970 Apr;117(2):341-6. doi: 10.1042/bj1170341.
9
The amino acid sequence around the active-site cysteine and histidine residues, and the buried cysteine residue in ficin.
Biochem J. 1970 Apr;117(2):333-40. doi: 10.1042/bj1170333.
10
Reactivities of the various protonic states in the reactions of papain and of L-cysteine with 2,2'- and with 4,4'- dipyridyl disulphide: evidence for nucleophilic reactivity in the un-ionized thiol group of the cysteine-25 residue of papain occasioned by its interaction with the histidine-159-asparagine-175 hydrogen-bonded system.
Biochem J. 1972 Jun;128(2):471-4. doi: 10.1042/bj1280471.
本文引用的文献
1
PAPAIN-CATALYSED HYDROLYSIS OF SOME HIPPURIC ESTERS. A NEW MECHANISM FOR PAPAIN-CATALYSED HYDROLYSIS.
Biochem J. 1965 Jul;96(1):199-204. doi: 10.1042/bj0960199.
2
A STUDY OF SOME THIOL ESTER HYDROLYSES AS MODELS FOR THE DEACYLATION STEP OF PAPAIN-CATALYSED HYDROLYSES.
Biochem J. 1965 Jul;96(1):194-8. doi: 10.1042/bj0960194.
3
DIRECT EVIDENCE FOR AN ACYLATED THIOL AS AN INTERMEDIATE IN PAPAIN- AND FICIN-CATALYSED HYDROLYSES.
Biochem J. 1965 Jul;96(1):189-93. doi: 10.1042/bj0960189.
4
KINETICS OF PAPAIN-CATALYZED HYDROLYSIS OF ALPHA-N-BENZOYL-L-ARGININE ETHYL ESTER AND ALPHA-N-BENZOYL-L-ARGININAMIDE.
J Am Chem Soc. 1965 Jun 20;87:2728-37. doi: 10.1021/ja01090a034.
5
CURRENT STATUS OF THE STRUCTURE OF PAPAIN: THE LINEAR SEQUENCE, ACTIVE SULFHYDRYL GROUP, AND THE DISULFIDE BRIDGES.
Proc Natl Acad Sci U S A. 1964 Nov;52(5):1276-83. doi: 10.1073/pnas.52.5.1276.
6
ION-EXCHANGE CHROMATOGRAPHY OF AMINO-ACIDS: IMPROVEMENTS IN THE SINGLE COLUMN SYSTEM.
Nature. 1964 Aug 1;203:483-4. doi: 10.1038/203483a0.
7
Alkylation and identification of the histidine residues at the active site of ribonuclease.
J Biol Chem. 1963 Jul;238:2413-9.
8
Phenolic hydroxyl ionization in papain.
J Biol Chem. 1961 Nov;236:2948-51.
9
The oxidation of ribonuclease with performic acid.
J Biol Chem. 1956 Apr;219(2):611-21.
10
Crystalline papain. I. Preparation, specificity, and activation.
J Biol Chem. 1954 Apr;207(2):515-31.
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