PMID:3486673: Difference between revisions

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<span style = 'font-size: large'> '''Frick, L, Wolfenden, R, Smal, E and Baker, DC'''  (1986) Transition-state stabilization by adenosine deaminase: structural studies of its inhibitory complex with deoxycoformycin.''Biochemistry'' '''25''':1616-21</span>
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!align=left  |Citation
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'''No author listed'''  (1986) Transition-state stabilization by adenosine deaminase: structural studies of its inhibitory complex with deoxycoformycin. ''Biochemistry'' '''25''':1616-21
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!align=left  |Abstract
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Experiments with radioactive deoxycoformycin indicate that the inhibitor is released from calf intestinal adenosine deaminase after the enzyme-inhibitor complex is disrupted by denaturation. Experiments with 2H2O and H218O indicate that the enzyme does not catalyze elimination-addition reactions that could have led to reversible covalent derivatization of the enzyme. Ultraviolet difference spectra and the influence of pH on inhibitor binding indicate that deoxycoformycin is bound intact as the neutral species, at a binding site that is less polar than solvent water. The enzyme-inhibitor complex appears to be held together by hydrogen bonds of extraordinary stability (ca. 10 kcal/mol). These results suggest that deamination proceeds by direct water attack, the enzyme acting as a general-base catalyst.
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=3486673 PubMed]


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|{{TableHeadingColor}} |'''Abstract''' || <protect>Experiments with radioactive deoxycoformycin indicate that the inhibitor is released from calf intestinal adenosine deaminase after the enzyme-inhibitor complex is disrupted by denaturation. Experiments with 2H2O and H218O indicate that the enzyme does not catalyze elimination-addition reactions that could have led to reversible covalent derivatization of the enzyme. Ultraviolet difference spectra and the influence of pH on inhibitor binding indicate that deoxycoformycin is bound intact as the neutral species, at a binding site that is less polar than solvent water. The enzyme-inhibitor complex appears to be held together by hydrogen bonds of extraordinary stability (ca. 10 kcal/mol). These results suggest that deamination proceeds by direct water attack, the enzyme acting as a general-base catalyst.</protect>
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|{{TableHeadingColor}} nowrap |'''Links''' ||  [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=3486673 PubMed]<br/>
Adenosine Deaminase Inhibitors; Animals; Cattle; Coformycin/analogs & derivatives; Coformycin/pharmacology; Drug Stability; Hydrogen-Ion Concentration; Intestines/enzymology; Kinetics; Ligands; Nucleoside Deaminases/antagonists & inhibitors; Pentostatin; Protein Binding; Ribonucleosides/pharmacology; Spectrophotometry, Ultraviolet
 
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==Significance {{HelpIcon|Help:Literature}} ==
==Significance {{HelpIcon|Help:Literature}} ==
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{{LitSignificance}}

Revision as of 19:25, 1 September 2013

Citation

No author listed (1986) Transition-state stabilization by adenosine deaminase: structural studies of its inhibitory complex with deoxycoformycin. Biochemistry 25:1616-21

Abstract

Experiments with radioactive deoxycoformycin indicate that the inhibitor is released from calf intestinal adenosine deaminase after the enzyme-inhibitor complex is disrupted by denaturation. Experiments with 2H2O and H218O indicate that the enzyme does not catalyze elimination-addition reactions that could have led to reversible covalent derivatization of the enzyme. Ultraviolet difference spectra and the influence of pH on inhibitor binding indicate that deoxycoformycin is bound intact as the neutral species, at a binding site that is less polar than solvent water. The enzyme-inhibitor complex appears to be held together by hydrogen bonds of extraordinary stability (ca. 10 kcal/mol). These results suggest that deamination proceeds by direct water attack, the enzyme acting as a general-base catalyst.

Links

PubMed

Keywords

Adenosine Deaminase Inhibitors; Animals; Cattle; Coformycin/analogs & derivatives; Coformycin/pharmacology; Drug Stability; Hydrogen-Ion Concentration; Intestines/enzymology; Kinetics; Ligands; Nucleoside Deaminases/antagonists & inhibitors; Pentostatin; Protein Binding; Ribonucleosides/pharmacology; Spectrophotometry, Ultraviolet

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Useful Materials and Methods

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Annotations

Gene product Qualifier GO ID GO term name Evidence Code with/from Aspect Notes Status

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GO:0005488

binding

IDA: Inferred from Direct Assay

CHEBI:27834

F

Add activity is inhibited by deoxycoformycin

complete

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