{c}
{tag=Work by V. Sideraki}
{tag=Work by David K. Wilson}
{tag=Work by Linda C. Kurz}
{tag=Work by Florante A. Quiocho}
{tag=Work by Frederick B. Rudolph}
{title2=1996}

https://doi.org/10.1021/bi961427e

Biochemistry 35, 15019–15028. <purine>-riboside hydration, spectroscopy and crystallography demonstrate why a loss of catalytic activity does not uniquely identify the residue that generates <hydroxide>.


Site-directed mutagenesis of histidine 238 in mouse adenosine deaminase: substitution of histidine 238 does not impede hydroxylate formation by V. Sideraki and others

 Discussion on "Site-directed mutagenesis of histidine 238 in mouse adenosine deaminase: substitution of histidine 238 does not impede hydroxylate formation by V. Sideraki and others" by Codex (@codex,  0)