3.1.3.37: sedoheptulose-bisphosphatase

This is an abbreviated version!
For detailed information about sedoheptulose-bisphosphatase, go to the full flat file.

Reaction

Synonyms

At3g55800, BiBPase, bifunctional fructose-1,6-bisphosphatase/sedoheptulose-1,7-bisphosphatase, dual-function fructose-1,6/sedoheptulose-1,7-bisphosphatase, FBP/SBPase, FBPase/SBPase, fructose -1,6-/sedoheptulose-1,7-bisphosphatase, fructose-1,6-/sedoheptulose-1,7-bisphoshatase, fructose-1,6-/sedoheptulose-1,7-bisphosphatase, fructose-1,6-biphosphatase/sedoheptulose-1,7-biphosphatase, fructose-1,6/sedoheptulose-1,7-bisphosphatase, GlpXp, More, ore, Os04g0234600, phosphatase, sedoheptulose di-, SBPase, SBPase3, SebP1, SED(1,7)P2ASE, sedoheptulose 1,7-bisphosphatase, sedoheptulose 1,7-diphosphatase, sedoheptulose 1,7-diphosphate phosphatase, sedoheptulose bisphosphatase, sedoheptulose diphosphatase, sedoheptulose-1,7-bisphosphatase, sedoheptulose-1-7 bisphosphatase, Sedoheptulose-bisphosphatase, SedP2-ase, seduheptulose bisphosphatase, SYNPCC7002_A1301, tll1276

ECTree

     3 Hydrolases

         3.1 Acting on ester bonds

             3.1.3 Phosphoric-monoester hydrolases

                3.1.3.37 sedoheptulose-bisphosphatase

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Results	in table
23	Activating Compound
700	AA Sequence
3	Application
1	CAS Registry Number
23	Cloned(Commentary)
4	Crystallization (Commentary)
2	Expression
20	General Information
1	General Stability
56	Inhibitors
1	kcat/KM [mM/s]
1	Ki Value [mM]
13	KM Value [mM]
41	Localization
13	Metals/Ions
16	Molecular Weight [Da]
38	Natural Substrates/ Products (Substrates)
135	Organism
3	Oxidation Stability
6	Pathway
17	PDB ID
11	pH Optimum
1	pH Range
1	pI Value
1	Posttranslational Modification
22	Protein Variants
13	Purification (Commentary)
1	Reaction
1	Reaction Type
80	Reference
37	Source Tissue
11	Specific Activity [micromol/min/mg]
1	Storage Stability
98	Substrates and Products (Substrate)
14	Subunits
92	Synonyms
1	Systematic Name
3	Temperature Optimum [°C]
5	Turnover Number [1/s]

Crystallization

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Crystallization on EC 3.1.3.37 - sedoheptulose-bisphosphatase

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

-

Synechococcus sp.

-

649161

hanging drop vapor diffusion method, using 100 mM HEPES, pH 7.5, 1.6 M ammonium sulfate, 7-9% (v/v) glycerol

Synechocystis sp.

P73922

729720

purified enzyme with bound sedoheptulose-7-phosphate in the absence of AMP, hanging drop vapour diffusion method, mixing of 0.001 ml of 15 mg/ml protein in 50 mM Tris-HCl pH 7.9, 50 mM NaCl, 1 mM Mg-sedoheptulose-7-phosphate, and 0.2 M MgCl2, with 0.001 ml of reservoir solution containing 0.06 M Na HEPES pH 7.5, 0.12 M MgCl2, and 27% v/v PEG 400, and equilibration over 0.1 ml of reservoir solution, X-ray diffraction structure determination and analysis at 2.34 A resolution

Thermosynechococcus vestitus

Q8DJE9

749507

structure with sedoheptulose-7-phosphate bound and in the absence of AMP, space group I4122. In the absence of AMP, the AMP-binding region is disordered

Thermosynechococcus vestitus

Q8DJE9

749507