Assignment of function to histidines 260 and 298 by engineering the E1 component of the Escherichia coli 2-oxoglutarate dehydrogenase complex; Substitutions that lead to acceptance of substrates lacking the 5-carboxyl group
Document Type
Article
Publication Date
9-6-2011
Abstract
The first component (E1o) of the Escherichia coli 2-oxoglutarate dehydrogenase complex (OGDHc) was engineered to accept substrates lacking the 5-carboxylate group by subjecting H260 and H298 to saturation mutagenesis. Apparently, H260 is required for substrate recognition, but H298 could be replaced with hydrophobic residues of similar molecular volume. To interrogate whether the second component would allow synthesis of acyl-coenzyme A derivatives, hybrid complexes consisting of recombinant components of OGDHc (o) and pyruvate dehydrogenase (p) enzymes were constructed, suggesting that a different component is the "gatekeeper" for specificity for these two multienzyme complexes in bacteria, E1p for pyruvate but E2o for 2-oxoglutarate. © 2011 American Chemical Society.
Identifier
80052213490 (Scopus)
Publication Title
Biochemistry
External Full Text Location
https://doi.org/10.1021/bi200936n
e-ISSN
15204995
ISSN
00062960
PubMed ID
21809826
First Page
7705
Last Page
7709
Issue
35
Volume
50
Grant
R01GM050380
Fund Ref
National Institute of General Medical Sciences
Recommended Citation
Shim, Da Jeong; Nemeria, Natalia S.; Balakrishnan, Anand; Patel, Hetalben; Song, Jaeyoung; Wang, Junjie; Jordan, Frank; and Farinas, Edgardo T., "Assignment of function to histidines 260 and 298 by engineering the E1 component of the Escherichia coli 2-oxoglutarate dehydrogenase complex; Substitutions that lead to acceptance of substrates lacking the 5-carboxyl group" (2011). Faculty Publications. 11182.
https://digitalcommons.njit.edu/fac_pubs/11182
