Cheryl Ingram-Smith, Kerry S. Smith
Adenosine monophosphate (AMP)-forming acetyl-CoA synthetase (ACS; acetate:CoA ligase (AMP-forming), EC 6.2.1.1) is a key enzyme for conversion of acetate to acetyl-CoA, an essential intermediate at...
Urkinase: Structure of Acetate Kinase, a Member of the ASKHA Superfamily of Phosphotransferases
Buss, Kathryn A., Cooper, David R., Ingram-Smith, Cheryl, Ferry, James G., Sanders, David Avram, Hasson, Miriam S.
Acetate kinase, an enzyme widely distributed in the Bacteria and Archaea domains, catalyzes the phosphorylation of acetate. We have determined the three-dimensional structure of Methanosarcina...
Urkinase: Structure of Acetate Kinase, a Member of the ASKHA Superfamily of Phosphotransferases
Buss, Kathryn A., Cooper, David R., Ingram-Smith, Cheryl, Ferry, James G., Sanders, David Avram, Hasson, Miriam S.
Wang, Ping, Ingram-Smith, Cheryl, Hadley, Jill A., Miller, Karen J.
Periplasmic cyclic β-glucans of Rhizobium species provide important functions during plant infection and hypo-osmotic adaptation. In Sinorhizobium meliloti (also known as Rhizobium meliloti), these...
Ingram-Smith, Cheryl, Miller, Karen J.
The cyclic β-(1,2)-glucans of Rhizobium meliloti and Agrobacterium tumefaciens play an important role during hypoosmotic adaptation, and the synthesis of these compounds is osmoregulated....
Identification of Essential Glutamates in the Acetate Kinase from Methanosarcina thermophila
Singh-Wissmann, Kavita, Ingram-Smith, Cheryl, Miles, Rebecca D., Ferry, James G.
Acetate kinase catalyzes the reversible phosphorylation of acetate (CH3COO− + ATP⇄CH3CO2PO32− + ADP). A mechanism which involves a covalent phosphoryl-enzyme intermediate has been proposed, and...
Identification of Essential Glutamates in the Acetate Kinase from Methanosarcina thermophila
Singh-Wissmann, Kavita, Ingram-Smith, Cheryl, Miles, Rebecca D., Ferry, James G.
Smith, Kerry S., Ingram-Smith, Cheryl, Ferry, James G.
The roles of an aspartate and an arginine, which are completely conserved in the active sites of β-class carbonic anhydrases, were investigated by steady-state kinetic analyses of replacement...
The Genome of M. acetivorans Reveals Extensive Metabolic and Physiological Diversity
Galagan, James E., Nusbaum, Chad, Roy, Alice, Endrizzi, Matthew G., Macdonald, Pendexter, FitzHugh, Will, ...
Methanogenesis, the biological production of methane, plays a pivotal role in the global carbon cycle and contributes significantly to global warming. The majority of methane in nature is derived...
Characterization of the Acetate Binding Pocket in the Methanosarcina thermophila Acetate Kinase
Ingram-Smith, Cheryl, Gorrell, Andrea, Lawrence, Sarah H., Iyer, Prabha, Smith, Kerry, Ferry, James G.
Acetate kinase catalyzes the reversible magnesium-dependent synthesis of acetyl phosphate by transfer of the ATP γ-phosphoryl group to acetate. Inspection of the crystal structure of the...
Characterization of the Acetate Binding Pocket in the Methanosarcina thermophila Acetate Kinase
Ingram-Smith, Cheryl, Gorrell, Andrea, Lawrence, Sarah H., Iyer, Prabha, Smith, Kerry, Ferry, James G.
Urkinase: Structure of Acetate Kinase, a Member of the ASKHA Superfamily of Phosphotransferases
Buss, Kathryn A., Cooper, David R., Ingram-Smith, Cheryl, Ferry, James G., Sanders, David Avram, Hasson, Miriam S.
Acetate kinase, an enzyme widely distributed in the Bacteria and Archaea domains, catalyzes the phosphorylation of acetate. We have determined the three-dimensional structure of Methanosarcina...
Urkinase: Structure of Acetate Kinase, a Member of the ASKHA Superfamily of Phosphotransferases
Buss, Kathryn A., Cooper, David R., Ingram-Smith, Cheryl, Ferry, James G., Sanders, David Avram, Hasson, Miriam S.
Wang, Ping, Ingram-Smith, Cheryl, Hadley, Jill A., Miller, Karen J.
Periplasmic cyclic β-glucans of Rhizobium species provide important functions during plant infection and hypo-osmotic adaptation. In Sinorhizobium meliloti (also known as Rhizobium meliloti), these...
Ingram-Smith, Cheryl, Miller, Karen J.
The cyclic β-(1,2)-glucans of Rhizobium meliloti and Agrobacterium tumefaciens play an important role during hypoosmotic adaptation, and the synthesis of these compounds is osmoregulated....
Identification of Essential Glutamates in the Acetate Kinase from Methanosarcina thermophila
Singh-Wissmann, Kavita, Ingram-Smith, Cheryl, Miles, Rebecca D., Ferry, James G.
Acetate kinase catalyzes the reversible phosphorylation of acetate (CH3COO− + ATP⇄CH3CO2PO32− + ADP). A mechanism which involves a covalent phosphoryl-enzyme intermediate has been proposed, and...
Identification of Essential Glutamates in the Acetate Kinase from Methanosarcina thermophila
Singh-Wissmann, Kavita, Ingram-Smith, Cheryl, Miles, Rebecca D., Ferry, James G.
Smith, Kerry S., Ingram-Smith, Cheryl, Ferry, James G.
The roles of an aspartate and an arginine, which are completely conserved in the active sites of β-class carbonic anhydrases, were investigated by steady-state kinetic analyses of replacement...
The Genome of M. acetivorans Reveals Extensive Metabolic and Physiological Diversity
Galagan, James E., Nusbaum, Chad, Roy, Alice, Endrizzi, Matthew G., Macdonald, Pendexter, FitzHugh, Will, ...
Methanogenesis, the biological production of methane, plays a pivotal role in the global carbon cycle and contributes significantly to global warming. The majority of methane in nature is derived...
Characterization of the Acetate Binding Pocket in the Methanosarcina thermophila Acetate Kinase
Ingram-Smith, Cheryl, Gorrell, Andrea, Lawrence, Sarah H., Iyer, Prabha, Smith, Kerry, Ferry, James G.
Acetate kinase catalyzes the reversible magnesium-dependent synthesis of acetyl phosphate by transfer of the ATP γ-phosphoryl group to acetate. Inspection of the crystal structure of the...
Characterization of the Acetate Binding Pocket in the Methanosarcina thermophila Acetate Kinase
Ingram-Smith, Cheryl, Gorrell, Andrea, Lawrence, Sarah H., Iyer, Prabha, Smith, Kerry, Ferry, James G.
AMP-forming acetyl-CoA synthetases in Archaea show unexpected diversity in substrate utilization
Ingram-Smith, Cheryl, Smith, Kerry S.
Adenosine monophosphate (AMP)-forming acetyl-CoA synthetase (ACS; acetate:CoA ligase (AMP-forming), EC 6.2.1.1) is a key enzyme for conversion of acetate to acetyl-CoA, an essential intermediate at...