PMID:3486673: Difference between revisions

From EcoliWiki
Jump to navigation Jump to search
imported>Wikientrybot
change PMID template to TableEdit version
imported>Wikientrybot
replace GO_table_reference with annotationlinks
Line 38: Line 38:


==Annotations {{HelpIcon|Help:Literature}}==
==Annotations {{HelpIcon|Help:Literature}}==
<protect><!--box uid=63ce1649aab8b3180235b0af7618f667.148920.E490f69a77d984-->
<protect><annotationlinks/></protect>
<!--
******************************************************************************************
*
*  ** PLEASE DON'T EDIT THIS TABLE DIRECTLY.  Use the edit table link under the table. **
*
****************************************************************************************** -->
{|  id="E490f69a77d984"  class=" tableEdit GO_table_reference" 
|- {{table heading style}}
!|Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status
|-
|
Add
|
 
|
GO:0005488
|
binding
|
IDA: Inferred from Direct Assay
|
CHEBI:27834
|
F
|
Add activity is inhibited by deoxycoformycin
|
complete
 
|- class="tableEdit_footer"
|<span class="tableEdit_editLink plainlinks">[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=63ce1649aab8b3180235b0af7618f667.148920.E490f69a77d984&page=148920&pagename={{FULLPAGENAMEE}}&type=0&template=GO_table_reference edit table]</span> || || || || || || || ||
|}
<!--box uid=63ce1649aab8b3180235b0af7618f667.148920.E490f69a77d984--></protect>


==EcoliWiki Links {{HelpIcon|Help:Literature}} ==
==EcoliWiki Links {{HelpIcon|Help:Literature}} ==

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

Significance

You can help EcoliWiki by summarizing why this paper is useful

Useful Materials and Methods

You can help Ecoliwiki by describing the useful materials (strains, plasmids, antibodies, etc) described in this paper.

Annotations

<annotationlinks/>

EcoliWiki Links

Add links to pages that link here (e.g. gene, product, method pages)

See also

References