3.5.99.6: glucosamine-6-phosphate deaminase

This is an abbreviated version!
For detailed information about glucosamine-6-phosphate deaminase, go to the full flat file.

Reaction

Synonyms

2-amino-2-deoxy-D-glucose-6-phosphate aminohydrolase (ketol-isomerizing), 2-amino-2-deoxy-D-glucose-6-phosphate ketol isomerase (deaminating), aminodeoxyglucosephosphate isomerase, cGNPDA2-a, cGNPDA2-b, cGNPDA2-c, cGNPDA2-d, EC 5.3.1.10, GlcN-6-P isomerase, GlcN6P deaminase, glucosamine 6-phosphate deaminase, glucosamine 6-phosphate isomerase, glucosamine phosphate deaminase, glucosamine-6-phosphate deaminase, glucosamine-6-phosphate deaminase 1, glucosamine-6-phosphate deaminase 2, glucosamine-6-phosphate deaminase 2 isoform 2, glucosamine-6-phosphate deaminase 2 isoform 3, glucosamine-6-phosphate isomerase, glucosamine-6P deaminase, glucosamine-P isomerase, glucosaminephosphate isomerase, gnd, GNPDA, GNPDA1, GNPDA2, isomerase, glucosamine phosphate, More, NAG1, NagB, NagBBs, NagBEc, oscillin, phoshoglucosamine isomerase, phosphoglucosaminisomerase, SMU.636 protein

ECTree

     3 Hydrolases

         3.5 Acting on carbon-nitrogen bonds, other than peptide bonds

             3.5.99 In other compounds

                3.5.99.6 glucosamine-6-phosphate deaminase

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Results	in table
32	Activating Compound
20207	AA Sequence
1	CAS Registry Number
16	Cloned(Commentary)
7	Crystallization (Commentary)
118	Disease/ Diagnostics
1	Expression
17	General Information
6	General Stability
37	Inhibitors
3	kcat/KM [mM/s]
14	Ki Value [mM]
99	KM Value [mM]
9	Metals/Ions
18	Molecular Weight [Da]
26	Natural Substrates/ Products (Substrates)
82	Organism
8	Pathway
53	PDB ID
23	pH Optimum
8	pH Range
1	pH Stability
3	pI Value
2	Posttranslational Modification
32	Protein Variants
22	Purification (Commentary)
7	Reaction
2	Reaction Type
63	Reference
38	Source Tissue
14	Specific Activity [micromol/min/mg]
7	Storage Stability
71	Substrates and Products (Substrate)
23	Subunits
72	Synonyms
1	Systematic Name
8	Temperature Optimum [°C]
2	Temperature Range [°C]
5	Temperature Stability [°C]
48	Turnover Number [1/s]

Crystallization

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Crystallization on EC 3.5.99.6 - glucosamine-6-phosphate deaminase

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

-

Escherichia coli

-

648235

structure of the enzyme in complexes with its allosteric activator and with a competitive inhibitor

Escherichia coli

-

648229

the crystallographic structure of F174A is determinated

Escherichia coli

-

648244

the structure of five complexes of the enzyme in R and T state is described and their kinetic and allosteric implication analysed, the ligand-free enzyme, T-conformer, undergoes an allosteric transition to the free active-site R conformer upon binding of the allosteric activator

Escherichia coli

P0A759

648240

-

Homo sapiens

P46926

648241

isozyme GNPDA1, X-ray diffraction structure determination and analysis at 1.75 A resolution

Homo sapiens

P46926, Q8TDQ7

718986

purified recombinant His-tagged enzyme, the protein solution contains 10 mg/ml protein in 20 mM Tris-HCl, 150 mM NaCl, pH 7.5, mixing of 0.001 ml of protein and 0.001 ml of reservoir solution, and equilibration against 0.5 ml of reservoir solution, hanging drop vapour diffusion method, X-ray diffraction structure determination and anaylsis at 2.4 A resolution

Streptococcus mutans

-

684212