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Literature summary for 4.1.2.13 extracted from

  • Zhang, L.; Guo, Z.; Huang, J.; Liu, M.; Wang, Y.; Ji, C.
    Expression, purification, crystallization and preliminary X-ray crystallographic analysis of fructose-1,6-bisphosphate aldolase from Escherichia coli (2014), Acta Crystallogr. F Struct. Biol. Commun., 70, 1376-1379 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
overexpression in Escherichia coli Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
crystals of recombinant fructose-1,6-bisphosphate aldolase class I are obtained by the sitting-drop vapour-diffusion technique in a condition consisting of 19 mg/ml FBPA I in 0.1 M Tris pH 9.0, 10% (w/v) polyethylene glycol 8000 and diffract to 2.0 A resolution. The crystals belong to the monoclinic space group C2, with unit-cell parameters 217.7 A (a), 114.9 A (b), 183.9 A (c), 124.6° (beta) Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Escherichia coli

Synonyms

Synonyms Comment Organism
FBPA I
-
Escherichia coli
fructose-1,6-bisphosphate aldolase
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Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
57
-
-
Escherichia coli

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
55
-
12 h, enzyme retains almost 100% activity Escherichia coli