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Your search keyword '"Da Jeong Shim"' showing total 2 results
Start Over Author "Da Jeong Shim" Journal biochemistry
2 results on '"Da Jeong Shim"'

1. 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

Author

Junjie Wang, Hetalben Patel, Jaeyoung Song, Frank Jordan, Natalia S. Nemeria, Anand Balakrishnan, Da Jeong Shim, and Edgardo T. Farinas

Subjects
chemistry.chemical_classification, Escherichia coli Proteins, Molecular Sequence Data, Protein engineering, Biology, Pyruvate dehydrogenase complex, medicine.disease_cause, Protein Engineering, Biochemistry, Article, Substrate Specificity, Enzyme, chemistry, medicine, Histidine, Ketoglutarate Dehydrogenase Complex, Amino Acid Sequence, Saturated mutagenesis, Branched-chain alpha-keto acid dehydrogenase complex, Escherichia coli, Peptide sequence
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.

Published
2011

2. Assignment of Function to Histidines 260 and 298 by Engineering the El Component of the Escherichia coil 2-Oxoglutarate Dehydrogenase Complex; Substitutions That Lead to Acceptance of Substrates Lacking the 5-Carboxyl Group.

Author

Da Jeong Shim, Nemeria, Natalia S., Balakrishnan, Anand, Patel, Hetalben, Song, Jaeyoung, Junjie Wang, Jordan, Frank, and Farinas, Edgardo T.

Subjects
*ESCHERICHIA coli, *DEHYDROGENASES, *CARBOXYLIC acids, *MUTAGENESIS, *PYRUVATES, *MULTIENZYME complexes
Abstract

The first component (Elo) of the Escherirhia coil 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 H-298 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' Elp foe pyruvate but E2o for 2-oxoglutarate. [ABSTRACT FROM AUTHOR]

Published
2011
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