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Literature summary for 3.5.99.6 extracted from

  • Rodionova, I.A.; Goodacre, N.; Babu, M.; Emili, A.; Uetz, P.; Saier, M.H.
    The nitrogen regulatory PII protein (GlnB) and N-acetylglucosamine 6-phosphate epimerase (NanE) allosterically activate glucosamine 6-phosphate deaminase (NagB) in Escherichia coli (2018), J. Bacteriol., 200, e00691_17 .
    View publication on PubMedView publication on EuropePMC
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Activating Compound

Activating Compound Comment Organism Structure
additional information NanE, GlcNAc-6P epimerase, and the uridylylated PII protein allosterically activate NagB by direct protein-protein interactions, overview. Uridylylated PII (but not underivatized PII) activates NagB about 10fold at low concentrations of substrate, whereas NanE increases NagB activity about 2fold. NanE activates NagB in the absence or presence of GlcNAc-6P, but histidine-phosphorylatable phosphocarrier protein (HPr) and U-PII activation requires the presence of GlcNAc-6P. NanE-dependent activation of NagB is not dependent on GlcNAc-6P. Activation of NagB by HPr and uridylylated PII, as well as by NanE and HPr (but not by NanE and U-PII), is synergistic, and the modeling, which suggests specific residues involved in complex formation, provides possible explanations. The uridylylated PII protein (U-PII) is generated by posttranslational modification under nitrogen-limiting conditions involving the glutamine/2-oxoglutarate ratio-sensing uridylyltransferase/uridylyl-removing enzyme GlnD. PII (GlnB)-dependent activation of NagB depends on the uridylylation state of GlnB, kinetics for NagB in the presence of PII at different stages of PII modification involving uridylylation by GlnD, overview. The effect is greater at pH 7.5 than at pH 8 due to the allosteric behavior of the Ser-1 mutant NagB, resulting from an increased Hill coefficient, also noticed for the wild-type NagB. Modeling of HPr/U-PII and of HPr/NanE binding to NagB. The PII protein is known to be a regulator of both the activity and the synthesis of glutamine synthetase (GlnA) in enteric bacteria, and of nitrogen metabolism in many other bacteria, archaea, and eukaryotes, in response to the availability of nitrogen sources Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information steady-state kinetics of NagB in presence or absence of activators, overview Escherichia coli
1.9
-
 alpha-D-glucosamine 6-phosphate pH 6.8, 30°C, 0.2 mM GlcNAc-6P, enzyme in absence of NanE Escherichia coli
2
-
 alpha-D-glucosamine 6-phosphate pH 6.8, 30°C, 0.2 mM GlcNAc-6P, enzyme in presence of NanE Escherichia coli
2.3
-
 alpha-D-glucosamine 6-phosphate pH 8.1, 30°C, 0.4 mM GlcNAc-6P, enzyme in presence of PII protein Escherichia coli
2.9
-
 alpha-D-glucosamine 6-phosphate pH 8.1, 30°C, 0.4 mM GlcNAc-6P, enzyme in absence of PII protein Escherichia coli
3.6
-
 alpha-D-glucosamine 6-phosphate pH 8.1, 30°C, 0.4 mM GlcNAc-6P, enzyme in presence of uridylylated PII protein Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
alpha-D-glucosamine 6-phosphate + H2O Escherichia coli
-
 D-fructose 6-phosphate + NH3
-
 ?
additional information Escherichia coli protein-protein interactions of HPr-NagB, U-PII-NagB, and NanE-NagB activate NagB by increasing the affinity of the enzyme for its substrate, GlcN-6P, and/or increasing the Vmax. NagB, glucosamine 6-phosphate deaminase. Protein-protein interactome for NagB, NagB interacts with numerous proteins in the Escherichia coli cell, overview ?
-
-

Organism

Organism UniProt Comment Textmining
Escherichia coli P0A759
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
alpha-D-glucosamine 6-phosphate + H2O
-
 Escherichia coli D-fructose 6-phosphate + NH3
-
 ?
additional information protein-protein interactions of HPr-NagB, U-PII-NagB, and NanE-NagB activate NagB by increasing the affinity of the enzyme for its substrate, GlcN-6P, and/or increasing the Vmax. NagB, glucosamine 6-phosphate deaminase. Protein-protein interactome for NagB, NagB interacts with numerous proteins in the Escherichia coli cell, overview Escherichia coli ?
-
-

Synonyms

Synonyms Comment Organism
NagB
-
 Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
 assay at Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5 8
-
 Escherichia coli

pH Range

pH Minimum pH Maximum Comment Organism
6 9 the pH dependency of NagB with a standard concentration of GlcNAc-6P, the kcat does not vary between pH 6.0 and pH 9.0. The Hill coefficient changes substantially with an optimum at pH 7.7 (Hill coefficient of 2.6), dropping below pH 7.0 or above pH 8.8. Results obtained at different pH values (pH 8.0, 7.8, 7.5, and 6.8) are in agreement with this statement Escherichia coli

General Information

General Information Comment Organism
metabolism NanE, GlcNAc-6P epimerase, and the uridylylated PII protein allosterically activate NagB by direct protein-protein interactions. NanE is essential for N-acetylneuraminic acid (NANA) and N-acetylmannosamine (ManNAc) utilization, and the PII protein is known to be a central metabolic nitrogen regulator. Regulatory links between carbon and nitrogen metabolism are important for adaptation of metabolism to different growth conditions. Regulatory interdependence between different metabolic pathways Escherichia coli
physiological function NagB, a glucosamine 6-phosphate deaminase in Escherichia coli, is essential for amino sugar utilization and is known to be allosterically regulated by N-acetylglucosamine 6-phosphate (GlcNAc-6P) and the histidine-phosphorylatable phosphocarrier protein, HPr. Specific physiological functions for the regulation of NagB by its three protein activators Escherichia coli