EC Number | Cloned (Comment) | Organism |
---|---|---|
2.3.1.157 | - |
Mycobacterium tuberculosis |
EC Number | Crystallization (Comment) | Organism |
---|---|---|
2.3.1.157 | structure of enzyme bound to ATP and N-acetyl-D-glucosamine 1-phosphate | Mycobacterium tuberculosis |
2.7.7.23 | purified enzyme complexed with ATP and N-acetyl-alpha-D-glucosamine 1-phosphate, soaking apo GlmUMtb crystals in soaking solution consisting of 10% PEG 8000, 100 mM HEPES, pH 7.5, 20 mM MgCl2, 4 mM CoCl2, 10 mM ATP, and 10 mM GlcNAc-1-P at 4°C, the ligand-bound crystals are cryoprotected in a cryosolution consisting of 20% ethylene glycol, 15% PEG 8000, 100 mM HEPES, pH 7.5, 20 mM MgCl2, and 4 mM CoCl2, X-ray diffraction structure determination and analysis at 1.98 A resolution | Mycobacterium tuberculosis |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
2.7.7.23 | ATP | the enzyme binds three magnesium ions and ATP at the active site, but shows no activity with ATP. ATP binding results in an inactive pre-catalytic enzymesubstrate complex, where it adopts an unusual conformation such that the reaction cannot be catalyzed | Mycobacterium tuberculosis | |
2.7.7.23 | additional information | displacement of MgB 2+ from its usual catalytically competent position, as noted in the crystal structure of RNA polymerase in an inactive state, is considered to be a key factor inhibiting the reaction. The entire metal-substrate complex renders the enzyme catalytically inactive | Mycobacterium tuberculosis |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
2.7.7.23 | Mg2+ | required, the enzyme utilizes two metal ions, MgA 2+ and MgB 2+, to catalyze the uridyltransfer reaction. The enzyme binds three magnesium ions and ATP at the active site. Displacement of MgB2+ from its usual catalytically competent position, as noted in the crystal structure of RNA polymerase in an inactive state, is considered to be a key factor inhibiting the reaction. In GlmUMtb[GlcNAc-1-P:ATP], the third metal ion, MgC2+ is also stabilized by one coordination interaction with Palpha and five coordination interactions with water molecules. Its coordination by Palpha results in the stabilization of an inactive conformation of ATP. Structure-function analysis, overview. The entire metal-substrate complex renders the enzyme catalytically inactive | Mycobacterium tuberculosis |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.7.7.23 | UTP + N-acetyl-alpha-D-glucosamine 1-phosphate | Mycobacterium tuberculosis | - |
diphosphate + UDP-N-acetyl-alpha-D-glucosamine | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.3.1.157 | Mycobacterium tuberculosis | P9WMN3 | - |
- |
2.3.1.157 | Mycobacterium tuberculosis ATCC 25618 | P9WMN3 | - |
- |
2.7.7.23 | Mycobacterium tuberculosis | - |
- |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.7.7.23 | additional information | enzyme GlmU is specific for its natural substrates UTP and N-acetyl-alpha-D-glucosamine 1-phosphate, substrate specificity, overview. No activity with ATP and TTP as well as glucose-1-phosphate and mannose-1-phosphate, very poor activity with GTP, low activity with CTP | Mycobacterium tuberculosis | ? | - |
? | |
2.7.7.23 | UTP + N-acetyl-alpha-D-glucosamine 1-phosphate | - |
Mycobacterium tuberculosis | diphosphate + UDP-N-acetyl-alpha-D-glucosamine | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
2.3.1.157 | bifunctional protein GlmU | - |
Mycobacterium tuberculosis |
2.7.7.23 | GlmU | - |
Mycobacterium tuberculosis |
2.7.7.23 | N-acetylglucosamine-1-phosphate uridyltransferase | - |
Mycobacterium tuberculosis |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
2.7.7.23 | 30 | - |
assay at | Mycobacterium tuberculosis |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
2.7.7.23 | 7.6 | - |
assay at | Mycobacterium tuberculosis |
EC Number | General Information | Comment | Organism |
---|---|---|---|
2.7.7.23 | evolution | the N-acetylglucosamine-1-phosphate uridyltransferase (GlmU) is a bifunctional enzyme exclusive to prokaryotes, that belongs to the family of sugar nucleotidyltransferases (SNTs) | Mycobacterium tuberculosis |
2.7.7.23 | physiological function | the enzyme binds N-acetylglucosamine-1-phosphate and UTP, and catalyzes an uridyltransfer reaction to synthesize UDP-GlcNAc, an important precursor for cell-wall biosynthesis | Mycobacterium tuberculosis |