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48:704–708
example, the αH80A/αH81A and αH80W/αH81W mutant
enzymes exhibited two significant structural changes in two
loop regions of the α-subunit (α74–82 and α152–155) that
affected the hydrogen-bonding interaction between αR157
and αCys104-SOH. Therefore, these studies indicate that a
combination of elements that include, the proper structure
of the active site (i.e. stabilization of active site nucleo-
phile through hydrogen-bonding), proper architecture of
the α-subunit, and outer-sphere residues (e.g. αHis80 and
αHis81), are necessary for NHase to efficiently catalyze
nitrile to amides.
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Acknowledgments This work was supported by the National Sci-
ence Foundation (CHE-1412443, RCH and CHE-1308672, DL). HC
gratefully acknowledges the ACS Project SEED for funding a summer
internship. GM/CA @ APS has been funded in whole or in part with
federal funds from the National Cancer Institute (ACB-12002) and
the National Institute of General Medical Sciences (AGM-12006).
28. Arakawa T, Kawano Y, Katayama Y, Nakayama H, Dohmae N,
Yohda M, Odaka M (2009) J Am Chem Soc 131:14838–14843
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