Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Vithani, N.; Bais, V.; Prakash, B.
    GlmU (N-acetylglucosamine-1-phosphate uridyltransferase) bound to three magnesium ions and ATP at the active site (2014), Acta Crystallogr. Sect. F, 70, 703-708.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.3.1.157
-
 Mycobacterium tuberculosis

Crystallization (Commentary)

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

Inhibitors

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 enzyme–substrate 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

Metals/Ions

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

Natural Substrates/ Products (Substrates)

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
-
 ?

Organism

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
-
-
-

Substrates and Products (Substrate)

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
-
 ?

Synonyms

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

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.7.7.23 30
-
 assay at Mycobacterium tuberculosis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.7.7.23 7.6
-
 assay at Mycobacterium tuberculosis

General Information

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