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Cheryl Ingram-Smith

Researcher at Pennsylvania State University

Publications -  14
Citations -  1016

Cheryl Ingram-Smith is an academic researcher from Pennsylvania State University. The author has contributed to research in topics: Acetate kinase & Methanosarcina thermophila. The author has an hindex of 9, co-authored 12 publications receiving 980 citations. Previous affiliations of Cheryl Ingram-Smith include University of Illinois at Urbana–Champaign & Washington University in St. Louis.

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Journal ArticleDOI

The Genome of M. Acetivorans Reveals Extensive Metabolic and Physiological Diversity

James E. Galagan, +76 more
- 01 Apr 2002 - 
TL;DR: The complete genome sequence of an acetate-utilizing methanogen, Methanosarcina acetivorans C2A, is reported, which indicates the likelihood of undiscovered natural energy sources for methanogenesis, whereas the presence of single-subunit carbon monoxide dehydrogenases raises the possibility of nonmethanogenic growth.
Journal ArticleDOI

Urkinase: Structure of Acetate Kinase, a Member of the ASKHA Superfamily of Phosphotransferases

TL;DR: Structural, biochemical, and geochemical considerations indicate that an acetate kinase may be the ancestral enzyme of the ASKHA (acetate and sugar kinases/Hsc70/actin) superfamily of phosphotransferases.
Journal ArticleDOI

Characterization of the Acetate Binding Pocket in the Methanosarcina thermophila Acetate Kinase

TL;DR: In this article, a solvent-accessible hydrophobic pocket formed by residues Val93, Leu122, Phe179, and Pro232 in the active site cleft was identified as a potential acetate binding site.
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Identification of Essential Glutamates in the Acetate Kinase from Methanosarcina thermophila

TL;DR: Alignment of the amino acid sequences for the acetate kinases from E. coli, Methanosarcina thermophila, and four other phylogenetically divergent microbes revealed high identity which included five glutamates, which indicates that neither residue is essential for catalysis or significantly influences the binding of acetate or ATP.
Journal ArticleDOI

Roles of the Conserved Aspartate and Arginine in the Catalytic Mechanism of an Archaeal β-Class Carbonic Anhydrase

TL;DR: The roles of an aspartate and an arginine, which are completely conserved in the active sites of beta-class carbonic anhydrases, were investigated by steady-state kinetic analyses of replacement variants of the beta- class enzyme (Cab) from the archaeon Methanobacterium thermoautotrophicum.