Abstract:
:Horse liver alcohol dehydrogenase was carboxymethylated at the active site Cys-46 using 90% [1-13C]bromoacetate. The enriched carboxylate resonance was studied in the absence and presence of coenzymes and inhibitors. Previous ambiguities regarding the resonance in the NAD+ complex have now been resolved. However, it is shown that imidazole, an inhibitor introduced during the carboxymethylation, is not removed by the standard gel filtration step frequently employed and must thus bind much more tightly to the enzyme than suspected. Competition experiments involving imidazole and halide inhibitors show that the imidazole is preferentially bound when both are present in equimolar amounts. This suggests that the crystallographically identified anion binding site at the zinc of the carboxymethylated enzyme may require re-evaluation. The electron density at the zinc of the modified enzyme may be better explained as being due to unsuspected binding of imidazole.
journal_name
Adv Exp Med Bioljournal_title
Advances in experimental medicine and biologyauthors
Jones DT,Khalifah RGdoi
10.1007/978-1-4757-1419-7_9subject
Has Abstractpub_date
1980-01-01 00:00:00pages
77-83eissn
0065-2598issn
2214-8019journal_volume
132pub_type
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