EC Number | Application | Comment | Organism |
---|---|---|---|
2.7.7.23 | medicine | potential target for antibacterial agents | Streptococcus pneumoniae |
2.7.7.23 | medicine | potential target for antibacterial agents | Escherichia coli |
EC Number | Cloned (Comment) | Organism |
---|---|---|
2.7.7.23 | expressed in M15 cells | Streptococcus pneumoniae |
EC Number | Crystallization (Comment) | Organism |
---|---|---|
2.3.1.157 | hanging-drop vapour-diffusion method. Crystal structures of the enzyme in unbound form, in complex with acetyl-coenzyme A and in complex with both AcCoA and the end product UDP-GlcNAc, determined and refined to 2.3, 2.5, and 1.75 A, respectively. GlmU molecule is organized in two separate domains connected via a long alpha-helical linker and associates as a trimer, with the 50-A-long left-handed beta-helix (LbH) C-terminal domains packed against each other in a parallel fashion and the C-terminal region extended far away from the LbH core and exchanged with the beta-helix from a neighboring subunit in the trimer. AcCoA binding induces the formation of a long and narrow tunnel, enclosed between two adjacent LbH domains and the interchanged C-terminal region of the third subunit, giving rise to an original active site architecture at the junction of three subunits | Streptococcus pneumoniae |
2.7.7.23 | recombinant enzyme, hanging drop vapor diffusion method | Streptococcus pneumoniae |
2.7.7.23 | recombinant enzyme, hanging drop vapor diffusion method | Escherichia coli |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.3.1.157 | D-glucosamine 1-phosphate + acetyl-CoA | Streptococcus pneumoniae | the bifunctional enzyme also possesses the activity of EC 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase and performs the last two steps in the synthesis of UDP-N-acetylglucosamine, which is an essential precursor in bacterial cell wall biosynthesis | N-acetyl-D-glucosamine 1-phosphate + CoA | - |
? | |
2.7.7.23 | diphosphate + UDP-N-acetyl-D-glucosamine | Streptococcus pneumoniae | amino sugar metabolism | UTP + N-acetyl-alpha-D-glucosamine 1-phosphate | - |
r | |
2.7.7.23 | diphosphate + UDP-N-acetyl-D-glucosamine | Escherichia coli | amino sugar metabolism | UTP + N-acetyl-alpha-D-glucosamine 1-phosphate | - |
r | |
2.7.7.23 | diphosphate + UDP-N-acetyl-D-glucosamine | Streptococcus pneumoniae | involved in synthesis of peptidoglycan and lipopolysaccharide | UTP + N-acetyl-alpha-D-glucosamine 1-phosphate | - |
r | |
2.7.7.23 | diphosphate + UDP-N-acetyl-D-glucosamine | Escherichia coli | involved in synthesis of peptidoglycan and lipopolysaccharide | UTP + N-acetyl-alpha-D-glucosamine 1-phosphate | - |
r |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.3.1.157 | Streptococcus pneumoniae | Q97R46 | - |
- |
2.7.7.23 | Escherichia coli | P0ACC7 | - |
- |
2.7.7.23 | Streptococcus pneumoniae | Q97R46 | - |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
2.7.7.23 | recombinant enzyme | Streptococcus pneumoniae |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.3.1.157 | D-glucosamine 1-phosphate + acetyl-CoA | the bifunctional enzyme also possesses the activity of EC 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase and performs the last two steps in the synthesis of UDP-N-acetylglucosamine, which is an essential precursor in bacterial cell wall biosynthesis | Streptococcus pneumoniae | N-acetyl-D-glucosamine 1-phosphate + CoA | - |
? | |
2.7.7.23 | diphosphate + UDP-N-acetyl-D-glucosamine | - |
Streptococcus pneumoniae | UTP + N-acetyl-alpha-D-glucosamine 1-phosphate | - |
r | |
2.7.7.23 | diphosphate + UDP-N-acetyl-D-glucosamine | - |
Escherichia coli | UTP + N-acetyl-alpha-D-glucosamine 1-phosphate | - |
r | |
2.7.7.23 | diphosphate + UDP-N-acetyl-D-glucosamine | amino sugar metabolism | Streptococcus pneumoniae | UTP + N-acetyl-alpha-D-glucosamine 1-phosphate | - |
r | |
2.7.7.23 | diphosphate + UDP-N-acetyl-D-glucosamine | amino sugar metabolism | Escherichia coli | UTP + N-acetyl-alpha-D-glucosamine 1-phosphate | - |
r | |
2.7.7.23 | diphosphate + UDP-N-acetyl-D-glucosamine | involved in synthesis of peptidoglycan and lipopolysaccharide | Streptococcus pneumoniae | UTP + N-acetyl-alpha-D-glucosamine 1-phosphate | - |
r | |
2.7.7.23 | diphosphate + UDP-N-acetyl-D-glucosamine | involved in synthesis of peptidoglycan and lipopolysaccharide | Escherichia coli | UTP + N-acetyl-alpha-D-glucosamine 1-phosphate | - |
r |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
2.7.7.23 | trimer | - |
Escherichia coli |
2.7.7.23 | trimer | crystal structure analysis | Streptococcus pneumoniae |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
2.3.1.157 | GlmU | bifunctional enzyme also possesses the activity of EC 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase | Streptococcus pneumoniae |
2.3.1.157 | N-acetylglucosamine-1-phosphate uridyltransferase | bifunctional enzyme also possesses the activity of EC 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase | Streptococcus pneumoniae |
2.7.7.23 | More | bifunctional enzyme with activity of: glucosamine-1-phosphate acetyltransferase and N-acetylglucosamine-1-phosphate uridyltransferase | Streptococcus pneumoniae |
2.7.7.23 | More | bifunctional enzyme with activity of: glucosamine-1-phosphate acetyltransferase and N-acetylglucosamine-1-phosphate uridyltransferase | Escherichia coli |