Malate synthase (MS) catalyses the aldol condensation of glyoxylate with acetyl-CoA to form malate as part of the second step of the glyoxylate bypass and an alternative to the tricarboxylic acid cycle in bacteria, fungi and plants. There have been i ...
Malate synthase (MS) catalyses the aldol condensation of glyoxylate with acetyl-CoA to form malate as part of the second step of the glyoxylate bypass and an alternative to the tricarboxylic acid cycle in bacteria, fungi and plants. There have been identified two isoforms, A and G (MSA and MSG, respectively) that differ in size and is attributed to an inserted alpha/beta domain in MSG that may have regulatory function [1,2]. In malate synthases, the TIM beta/alpha-barrel fold and the C-terminal domain are well conserved and the cleft between them forms the active site [1,2,3,4]. MSA and MSG consist of an N-terminal alpha-helical clasp domain, a central TIM barrel domain and a C-terminal helical plug domain. This is the TIM barrel domain of malate synthases.
Malate synthase (MS) catalyses the aldol condensation of glyoxylate with acetyl-CoA to form malate as part of the second step of the glyoxylate bypass and an alternative to the tricarboxylic acid cycle in bacteria, fungi and plants. There have been i ...
Malate synthase (MS) catalyses the aldol condensation of glyoxylate with acetyl-CoA to form malate as part of the second step of the glyoxylate bypass and an alternative to the tricarboxylic acid cycle in bacteria, fungi and plants. There have been identified two isoforms, A and G (MSA and MSG, respectively) that differ in size and is attributed to an inserted alpha/beta domain in MSG that may have regulatory function [1,2,3,4]. Members of the isoform G family are only found in bacteria. This entry represents the alpha/beta insertion domain from MSG, which buttressed one side of the TIM-barrel domain [1].
Malate synthase (MS) catalyses the aldol condensation of glyoxylate with acetyl-CoA to form malate as part of the second step of the glyoxylate bypass and an alternative to the tricarboxylic acid cycle in bacteria, fungi and plants. There have been i ...
Malate synthase (MS) catalyses the aldol condensation of glyoxylate with acetyl-CoA to form malate as part of the second step of the glyoxylate bypass and an alternative to the tricarboxylic acid cycle in bacteria, fungi and plants. There have been identified two isoforms, A and G (MSA and MSG, respectively) that differ in size and is attributed to an inserted alpha/beta domain in MSG that may have regulatory function [1,2]. In malate synthases, the TIM beta/alpha-barrel fold and the C-terminal helical domain are well conserved and the cleft between them forms the active site [1,2,3,4]. This entry represents the C-terminal domain which consists of a five-helix 'plug' connected to the barrel by an extended loop and caps the active site.
Malate synthase (MS) catalyses the aldol condensation of glyoxylate with acetyl-CoA to form malate as part of the second step of the glyoxylate bypass and an alternative to the tricarboxylic acid cycle in bacteria, fungi and plants. There have been i ...
Malate synthase (MS) catalyses the aldol condensation of glyoxylate with acetyl-CoA to form malate as part of the second step of the glyoxylate bypass and an alternative to the tricarboxylic acid cycle in bacteria, fungi and plants. There have been identified two isoforms, A and G (MSA and MSG, respectively) that differ in size and is attributed to an inserted alpha/beta domain in MSG that may have regulatory function [1,2]. They consist of an N-terminal alpha-helical claps, a central TIM barrel and a C-terminal alpha-helical plug. This entry represents the N-terminal clasp that wraps around one side of the TIM barrel and buttressed it [1,2,3,4].
