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Literature summary for 3.2.1.26 extracted from

  • Xie, J.; Hu, H.X.; Cai, K.; Xia, L.Y.; Yang, F.; Jiang, Y.L.; Chen, Y.; Zhou, C.Z.
    Structural and enzymatic analyses of Anabaena heterocyst-specific alkaline invertase InvB (2018), FEBS Lett., 592, 1589-1601 .
    View publication on PubMed
Search for more literature for 3.2.1.26

Cloned(Commentary)

Cloned (Comment) Organism
cloned into a pET29a-derived vector with an N-terminal His6 tag. Likewise, the truncated InvB covering residues Thr9-Ser457 is constructed for crystallization. Both the wild-type and mutant proteins are overexpressed in Escherichia coli strain BL21(DE3). Selenomethionine (SeMet)-substituted full-length and truncated InvB are overexpressed in Escherichia coli B834 (DE3) Nostoc sp. PCC 7120 = FACHB-418

Crystallization (Commentary)

Crystallization (Comment) Organism
both native and SeMet-substituted InvB are concentrated to 5-10 mg/ml by ultrafiltration for crystallization. Crystals are grown at 16°C using the hanging drop vapor diffusion method Nostoc sp. PCC 7120 = FACHB-418

Protein Variants

Protein Variants Comment Organism
R429A catalytic efficiency (kcat/Km) of the mutant enzyme is 9% compared to the catalytic efficiency of the wild-type enzyme Nostoc sp. PCC 7120 = FACHB-418
R429N catalytic efficiency (kcat/Km) of the mutant enzyme is 20% compared to the catalytic efficiency of the wild-type enzyme Nostoc sp. PCC 7120 = FACHB-418
R430A mutant enzyme shows no detectable activity Nostoc sp. PCC 7120 = FACHB-418
R430N catalytic efficiency (kcat/Km) of the mutant enzyme is 16% compared to the catalytic efficiency of the wild-type enzyme Nostoc sp. PCC 7120 = FACHB-418

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
8.9
-
 sucrose pH 7.7, 30°C, invertase InvB, wild-type enzyme Nostoc sp. PCC 7120 = FACHB-418
18.1
-
 sucrose pH 7.7, 30°C, invertase InvB, mutant enzyme R430N Nostoc sp. PCC 7120 = FACHB-418
20.8
-
 sucrose pH 7.9, 30°C, invertase InvA, wild-type enzyme Nostoc sp. PCC 7120 = FACHB-418
27.1
-
 sucrose pH 7.9, 30°C, invertase InvA, mutant enzyme R429N Nostoc sp. PCC 7120 = FACHB-418
89.3
-
 sucrose pH 7.9, 30°C, invertase InvA, mutant enzyme R429A Nostoc sp. PCC 7120 = FACHB-418

Organism

Organism UniProt Comment Textmining
Nostoc sp. PCC 7120 = FACHB-418 Q8YWS9
-
-
Nostoc sp. PCC 7120 = FACHB-418 Q8YYM9
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Nostoc sp. PCC 7120 = FACHB-418

Source Tissue

Source Tissue Comment Organism Textmining
heterocyst compared to invertase InvA, invertase InvB possesses a much higher catalytic activity. The higher activity may be responsible for the vital role of InvB in heterocyst development and nitrogen fixation Nostoc sp. PCC 7120 = FACHB-418
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
sucrose + H2O
-
 Nostoc sp. PCC 7120 = FACHB-418 beta-D-fructose + alpha-D-glucose
-
 ?
sucrose + H2O invertase InvB has a higher affinity toward sucrose and a higher catalytic efficiency (kcat/Km) of about five times to that of invertase InvA Nostoc sp. PCC 7120 = FACHB-418 beta-D-fructose + alpha-D-glucose
-
 ?

Synonyms

Synonyms Comment Organism
alkaline invertase InvA
-
 Nostoc sp. PCC 7120 = FACHB-418
alkaline invertase InvB
-
 Nostoc sp. PCC 7120 = FACHB-418

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
5.3
-
 sucrose pH 7.7, 30°C, invertase InvB, mutant enzyme R430N Nostoc sp. PCC 7120 = FACHB-418
18.9
-
 sucrose pH 7.9, 30°C, invertase InvA, mutant enzyme R429N Nostoc sp. PCC 7120 = FACHB-418
29.1
-
 sucrose pH 7.9, 30°C, invertase InvA, mutant enzyme R429A Nostoc sp. PCC 7120 = FACHB-418
73.7
-
 sucrose pH 7.9, 30°C, invertase InvA, wild-type enzyme Nostoc sp. PCC 7120 = FACHB-418
163.8
-
 sucrose pH 7.7, 30°C, invertase InvB, wild-type enzyme Nostoc sp. PCC 7120 = FACHB-418

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.7
-
-
 Nostoc sp. PCC 7120 = FACHB-418
7.9
-
-
 Nostoc sp. PCC 7120 = FACHB-418

pH Range

pH Minimum pH Maximum Comment Organism
7 9 pH 7.0: about 45% of maximal activity, pH 9.0: about 60% of maximal activity, invertase InvA Nostoc sp. PCC 7120 = FACHB-418
7 8.5 pH 7.0: about 40% of maximal activity, pH 8.5: about 65% of maximal activity, invertase InvB Nostoc sp. PCC 7120 = FACHB-418

General Information

General Information Comment Organism
physiological function compared to invertase InvA, invertase InvB possesses a much higher catalytic activity. The higher activity may be responsible for the vital role of InvB in heterocyst development and nitrogen fixation Nostoc sp. PCC 7120 = FACHB-418

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.33
-
 sucrose pH 7.9, 30°C, invertase InvA, mutant enzyme R429A Nostoc sp. PCC 7120 = FACHB-418
0.7
-
 sucrose pH 7.9, 30°C, invertase InvA, mutant enzyme R429N Nostoc sp. PCC 7120 = FACHB-418
2.9
-
 sucrose pH 7.7, 30°C, invertase InvB, mutant enzyme R430N Nostoc sp. PCC 7120 = FACHB-418
3.54
-
 sucrose pH 7.9, 30°C, invertase InvA, wild-type enzyme Nostoc sp. PCC 7120 = FACHB-418
18.4
-
 sucrose pH 7.7, 30°C, invertase InvB, wild-type enzyme Nostoc sp. PCC 7120 = FACHB-418