Pub. Date : 2003 Nov 1
PMID : 12940772
12 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | Serine acetyltransferase of Escherichia coli: substrate specificity and feedback control by cysteine. | Cysteine | streptothricin acetyltransferase | Escherichia coli |
| 2 | Although SAT (serine acetyltransferase) of Escherichia coli, which catalyses the first step in cysteine synthesis, proceeds via a random-order ternary complex reaction mechanism [Hindson and Shaw (2003) Biochemistry 42, 3113-3119], it has been suggested that the nearly identical enzyme from Salmonella typhimurium might involve an acetyl-enzyme intermediate [Leu and Cook (1994) Protein Peptide Lett. | Cysteine | streptothricin acetyltransferase | Escherichia coli |
| 3 | Although SAT (serine acetyltransferase) of Escherichia coli, which catalyses the first step in cysteine synthesis, proceeds via a random-order ternary complex reaction mechanism [Hindson and Shaw (2003) Biochemistry 42, 3113-3119], it has been suggested that the nearly identical enzyme from Salmonella typhimurium might involve an acetyl-enzyme intermediate [Leu and Cook (1994) Protein Peptide Lett. | Cysteine | streptothricin acetyltransferase | Escherichia coli |
| 4 | Since earlier kinetic studies with SAT from S. typhimurium suggested that cysteine competes with acetyl-CoA for binding, rather than serine with which it is isostructural, the specificity of the serine-binding pocket was assessed with three substrate mimics; beta-hydroxypropionic acid, glycine and ethanolamine. | Cysteine | streptothricin acetyltransferase | Escherichia coli |
| 5 | Since earlier kinetic studies with SAT from S. typhimurium suggested that cysteine competes with acetyl-CoA for binding, rather than serine with which it is isostructural, the specificity of the serine-binding pocket was assessed with three substrate mimics; beta-hydroxypropionic acid, glycine and ethanolamine. | Serine | streptothricin acetyltransferase | Escherichia coli |
| 6 | The data show that SAT interacts productively with the amino and hydroxymethyl moieties of serine, whereas the carboxyl group provides an essential contribution to binding strongly, supporting a view that cysteine will interact productively at the serine-binding site. | Serine | streptothricin acetyltransferase | Escherichia coli |
| 7 | The data show that SAT interacts productively with the amino and hydroxymethyl moieties of serine, whereas the carboxyl group provides an essential contribution to binding strongly, supporting a view that cysteine will interact productively at the serine-binding site. | Cysteine | streptothricin acetyltransferase | Escherichia coli |
| 8 | Such a proposal is supported by the results of micro-calorimetric studies which show that cysteine competes with serine for binding to SAT rather than with CoA. | Cysteine | streptothricin acetyltransferase | Escherichia coli |
| 9 | Such a proposal is supported by the results of micro-calorimetric studies which show that cysteine competes with serine for binding to SAT rather than with CoA. | Serine | streptothricin acetyltransferase | Escherichia coli |
| 10 | It follows that tight binding of cysteine at the serine-binding site near the catalytic centre may be the effector of a substantial reduction in the affinity of SAT for CoA, yielding the observed pattern of steady-state inhibition and the mechanism by which cysteine mediates effective end-product control of its synthesis. | Cysteine | streptothricin acetyltransferase | Escherichia coli |
| 11 | It follows that tight binding of cysteine at the serine-binding site near the catalytic centre may be the effector of a substantial reduction in the affinity of SAT for CoA, yielding the observed pattern of steady-state inhibition and the mechanism by which cysteine mediates effective end-product control of its synthesis. | Serine | streptothricin acetyltransferase | Escherichia coli |
| 12 | It follows that tight binding of cysteine at the serine-binding site near the catalytic centre may be the effector of a substantial reduction in the affinity of SAT for CoA, yielding the observed pattern of steady-state inhibition and the mechanism by which cysteine mediates effective end-product control of its synthesis. | Cysteine | streptothricin acetyltransferase | Escherichia coli |