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Literature summary extracted from

  • Ortiz-Soto, M.E.; Porras-Dominguez, J.R.; Seibel, J.; Lopez-Munguia, A.
    A close look at the structural features and reaction conditions that modulate the synthesis of low and high molecular weight fructans by levansucrases (2019), Carbohydr. Polym., 219, 130-142 .
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
2.4.1.10 D194N the mutant shows 8300fold decrease in catalytic efficiency compared to the wild type enzyme Zymomonas mobilis
2.4.1.10 D219A inactive Pseudomonas syringae
2.4.1.10 D247A inactive Bacillus subtilis
2.4.1.10 D257A inactive Priestia megaterium
2.4.1.10 D300A the mutant shows 2fold decrease in catalytic efficiency compared to the wild type enzyme Pseudomonas syringae
2.4.1.10 D300N the mutant shows 4fold decrease in catalytic efficiency compared to the wild type enzyme Pseudomonas syringae
2.4.1.10 D308N the mutant shows 3fold decrease in catalytic efficiency compared to the wild type enzyme Zymomonas mobilis
2.4.1.10 D333A the mutant shows 6fold decrease in catalytic efficiency compared to the wild type enzyme Pseudomonas syringae
2.4.1.10 D333N the mutant shows 2fold decrease in catalytic efficiency compared to the wild type enzyme Pseudomonas syringae
2.4.1.10 D62A inactive Pseudomonas syringae
2.4.1.10 D86A inactive Zymomonas mobilis
2.4.1.10 D86A inactive Bacillus subtilis
2.4.1.10 D95A inactive Priestia megaterium
2.4.1.10 E117Q the mutant shows 5fold decrease in catalytic efficiency compared to the wild type enzyme Zymomonas mobilis
2.4.1.10 E146Q the mutant shows 2fold decrease in catalytic efficiency compared to the wild type enzyme Pseudomonas syringae
2.4.1.10 E211Q the mutant shows 22fold decrease in catalytic efficiency compared to the wild type enzyme Zymomonas mobilis
2.4.1.10 E236Q the mutant shows 42fold decrease in catalytic efficiency compared to the wild type enzyme Pseudomonas syringae
2.4.1.10 E278D transfructosylation activity of the variant decreases 15% at 15°C as compared to the wild type enzyme Zymomonas mobilis
2.4.1.10 E278D transfructosylation activity of the variant increases 18% at 15°C as compared to the wild type enzyme Zymomonas mobilis
2.4.1.10 E303A inactive Pseudomonas syringae
2.4.1.10 E303Q inactive Pseudomonas syringae
2.4.1.10 E342A inactive Bacillus subtilis
2.4.1.10 E350A nearly inactive Priestia megaterium
2.4.1.10 E352A inactive Priestia megaterium
2.4.1.10 H243L the mutant shows 2fold decrease in catalytic efficiency compared to the wild type enzyme Bacillus subtilis
2.4.1.10 H296K the mutant shows 29fold decrease in catalytic efficiency compared to the wild type enzyme Zymomonas mobilis
2.4.1.10 H296L the mutant shows 41fold decrease in catalytic efficiency compared to the wild type enzyme Zymomonas mobilis
2.4.1.10 H296R the mutant shows 23fold decrease in catalytic efficiency compared to the wild type enzyme Zymomonas mobilis
2.4.1.10 H296S the mutant shows 77fold decrease in catalytic efficiency compared to the wild type enzyme Zymomonas mobilis
2.4.1.10 H296W the mutant shows 14fold decrease in catalytic efficiency compared to the wild type enzyme Zymomonas mobilis
2.4.1.10 H321K the mutant shows 75fold decrease in catalytic efficiency compared to the wild type enzyme Pseudomonas syringae
2.4.1.10 H321L the mutant shows 61fold decrease in catalytic efficiency compared to the wild type enzyme Pseudomonas syringae
2.4.1.10 H321R the mutant shows 82fold decrease in catalytic efficiency compared to the wild type enzyme Pseudomonas syringae
2.4.1.10 H321S the mutant shows 234fold decrease in catalytic efficiency compared to the wild type enzyme Pseudomonas syringae
2.4.1.10 I341V the mutant shows wild type catalytic efficiency Bacillus subtilis
2.4.1.10 K373A the mutant shows 2fold decrease in catalytic efficiency compared to the wild type enzyme Priestia megaterium
2.4.1.10 K373R the mutant shows 2fold decrease in catalytic efficiency compared to the wild type enzyme Priestia megaterium
2.4.1.10 N242H the mutant shows 31fold decrease in catalytic efficiency compared to the wild type enzyme Bacillus subtilis
2.4.1.10 N252A the mutant shows wild type activity Priestia megaterium
2.4.1.10 N252D the mutant shows wild type activity Priestia megaterium
2.4.1.10 N252G the mutant shows wild type activity Priestia megaterium
2.4.1.10 N252H the mutant shows 8fold decrease in catalytic efficiency compared to the wild type enzyme Priestia megaterium
2.4.1.10 Q301A the mutant shows 55fold decrease in catalytic efficiency compared to the wild type enzyme Pseudomonas syringae
2.4.1.10 Q301E the mutant shows 2fold decrease in catalytic efficiency compared to the wild type enzyme Pseudomonas syringae
2.4.1.10 R193H the mutant shows 298fold decrease in catalytic efficiency compared to the wild type enzyme Zymomonas mobilis
2.4.1.10 R193K the mutant shows 521fold decrease in catalytic efficiency compared to the wild type enzyme Zymomonas mobilis
2.4.1.10 R256A nearly inactive Priestia megaterium
2.4.1.10 R360H the mutant shows 5fold decrease in catalytic efficiency compared to the wild type enzyme. The mutant still can produce levan, but has 60% less transfructosylation activity Bacillus subtilis
2.4.1.10 R360K the mutant shows 1-4fold decrease in catalytic efficiency compared to the wild type enzyme Bacillus subtilis
2.4.1.10 R360S the mutant shows 98-226fold decrease in catalytic efficiency compared to the wild type enzyme Bacillus subtilis
2.4.1.10 R370A the mutant shows 57fold decrease in catalytic efficiency compared to the wild type enzyme Priestia megaterium
2.4.1.10 S164A the mutant shows 8fold decrease in catalytic efficiency compared to the wild type enzyme Bacillus subtilis
2.4.1.10 S173A the mutant shows 19fold decrease in catalytic efficiency compared to the wild type enzyme Priestia megaterium
2.4.1.10 S173G the mutant shows 59fold decrease in catalytic efficiency compared to the wild type enzyme Priestia megaterium
2.4.1.10 S173T the mutant shows 7fold decrease in catalytic efficiency compared to the wild type enzyme Priestia megaterium
2.4.1.10 S422A the mutant shows 4fold decrease in catalytic efficiency compared to the wild type enzyme Priestia megaterium
2.4.1.10 T302M the mutant shows wild type activity Pseudomonas syringae
2.4.1.10 T302P the mutant shows 3fold decrease in catalytic efficiency compared to the wild type enzyme Pseudomonas syringae
2.4.1.10 W118H the mutant shows 521fold decrease in catalytic efficiency compared to the wild type enzyme Zymomonas mobilis
2.4.1.10 W118N the mutant shows 521fold decrease in catalytic efficiency compared to the wild type enzyme Zymomonas mobilis
2.4.1.10 W172A the mutant shows 69fold decrease in catalytic efficiency compared to the wild type enzyme Priestia megaterium
2.4.1.10 W47H the mutant shows 695fold decrease in catalytic efficiency compared to the wild type enzyme Zymomonas mobilis
2.4.1.10 W47N the mutant shows 72fold decrease in catalytic efficiency compared to the wild type enzyme Zymomonas mobilis
2.4.1.10 W61A the mutant shows 137fold decrease in catalytic efficiency compared to the wild type enzyme Pseudomonas syringae
2.4.1.10 W61N the mutant shows 3708fold decrease in catalytic efficiency compared to the wild type enzyme Pseudomonas syringae
2.4.1.10 W94A the mutant shows 11fold decrease in catalytic efficiency compared to the wild type enzyme Priestia megaterium
2.4.1.10 Y247A the mutant shows 2fold decrease in catalytic efficiency compared to the wild type enzyme Priestia megaterium
2.4.1.10 Y247I the mutant shows 2fold decrease in catalytic efficiency compared to the wild type enzyme Priestia megaterium
2.4.1.10 Y247W the mutant shows 0.2fold decrease in catalytic efficiency compared to the wild type enzyme Priestia megaterium
2.4.1.10 Y421A the mutant shows 520fold decrease in catalytic efficiency compared to the wild type enzyme Priestia megaterium
2.4.1.10 Y421F the mutant shows 33fold decrease in catalytic efficiency compared to the wild type enzyme Priestia megaterium
2.4.1.10 Y421M the mutant shows 302fold decrease in catalytic efficiency compared to the wild type enzyme Priestia megaterium
2.4.1.10 Y421W the mutant shows 101fold decrease in catalytic efficiency compared to the wild type enzyme Priestia megaterium
2.4.1.10 Y429N the mutant shows 1015fold decrease in catalytic efficiency compared to the wild type enzyme Bacillus subtilis
2.4.1.10 Y439A the mutant shows 2130fold decrease in catalytic efficiency compared to the wild type enzyme Priestia megaterium
2.4.1.10 Y439F the mutant shows 9fold decrease in catalytic efficiency compared to the wild type enzyme Priestia megaterium
2.4.1.10 Y439M the mutant shows 131fold decrease in catalytic efficiency compared to the wild type enzyme Priestia megaterium
2.4.1.10 Y439W the mutant shows 41fold decrease in catalytic efficiency compared to the wild type enzyme Priestia megaterium

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.4.1.10 extracellular
-
 Zymomonas mobilis
-
-
2.4.1.10 extracellular
-
 Pseudomonas syringae
-
-
2.4.1.10 extracellular
-
 Bacillus subtilis
-
-
2.4.1.10 extracellular
-
 Priestia megaterium
-
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.4.1.10 sucrose + [beta-D-fructofuranosyl-(2->6)]n alpha-D-glucopyranoside Zymomonas mobilis
-
 D-glucose + [beta-D-fructofuranosyl-(2->6)]n+1 alpha-D-glucopyranoside
-
 ?
2.4.1.10 sucrose + [beta-D-fructofuranosyl-(2->6)]n alpha-D-glucopyranoside Pseudomonas syringae
-
 D-glucose + [beta-D-fructofuranosyl-(2->6)]n+1 alpha-D-glucopyranoside
-
 ?
2.4.1.10 sucrose + [beta-D-fructofuranosyl-(2->6)]n alpha-D-glucopyranoside Bacillus subtilis
-
 D-glucose + [beta-D-fructofuranosyl-(2->6)]n+1 alpha-D-glucopyranoside
-
 ?
2.4.1.10 sucrose + [beta-D-fructofuranosyl-(2->6)]n alpha-D-glucopyranoside Priestia megaterium
-
 D-glucose + [beta-D-fructofuranosyl-(2->6)]n+1 alpha-D-glucopyranoside
-
 ?
2.4.1.10 sucrose + [beta-D-fructofuranosyl-(2->6)]n alpha-D-glucopyranoside Bacillus subtilis 168
-
 D-glucose + [beta-D-fructofuranosyl-(2->6)]n+1 alpha-D-glucopyranoside
-
 ?
2.4.1.10 sucrose + [beta-D-fructofuranosyl-(2->6)]n alpha-D-glucopyranoside Priestia megaterium DSM 319
-
 D-glucose + [beta-D-fructofuranosyl-(2->6)]n+1 alpha-D-glucopyranoside
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.4.1.10 Bacillus subtilis P05655
-
-
2.4.1.10 Bacillus subtilis 168 P05655
-
-
2.4.1.10 Priestia megaterium D5DC07
-
-
2.4.1.10 Priestia megaterium DSM 319 D5DC07
-
-
2.4.1.10 Pseudomonas syringae
-
-
-
2.4.1.10 Zymomonas mobilis
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.1.10 sucrose + H2O
-
 Zymomonas mobilis D-glucose + D-fructose
-
 ?
2.4.1.10 sucrose + H2O
-
 Pseudomonas syringae D-glucose + D-fructose
-
 ?
2.4.1.10 sucrose + H2O
-
 Bacillus subtilis D-glucose + D-fructose
-
 ?
2.4.1.10 sucrose + H2O
-
 Priestia megaterium D-glucose + D-fructose
-
 ?
2.4.1.10 sucrose + H2O
-
 Bacillus subtilis 168 D-glucose + D-fructose
-
 ?
2.4.1.10 sucrose + H2O
-
 Priestia megaterium DSM 319 D-glucose + D-fructose
-
 ?
2.4.1.10 sucrose + sucrose
-
 Zymomonas mobilis 1-kestose + 6-kestose + neo-kestose + ?
-
 ?
2.4.1.10 sucrose + sucrose
-
 Pseudomonas syringae 1-kestose + 6-kestose + neo-kestose + ?
-
 ?
2.4.1.10 sucrose + sucrose
-
 Bacillus subtilis 1-kestose + 6-kestose + neo-kestose + ?
-
 ?
2.4.1.10 sucrose + sucrose
-
 Priestia megaterium 1-kestose + 6-kestose + neo-kestose + ?
-
 ?
2.4.1.10 sucrose + sucrose
-
 Bacillus subtilis 168 1-kestose + 6-kestose + neo-kestose + ?
-
 ?
2.4.1.10 sucrose + sucrose
-
 Priestia megaterium DSM 319 1-kestose + 6-kestose + neo-kestose + ?
-
 ?
2.4.1.10 sucrose + [beta-D-fructofuranosyl-(2->6)]n alpha-D-glucopyranoside
-
 Zymomonas mobilis D-glucose + [beta-D-fructofuranosyl-(2->6)]n+1 alpha-D-glucopyranoside
-
 ?
2.4.1.10 sucrose + [beta-D-fructofuranosyl-(2->6)]n alpha-D-glucopyranoside
-
 Pseudomonas syringae D-glucose + [beta-D-fructofuranosyl-(2->6)]n+1 alpha-D-glucopyranoside
-
 ?
2.4.1.10 sucrose + [beta-D-fructofuranosyl-(2->6)]n alpha-D-glucopyranoside
-
 Bacillus subtilis D-glucose + [beta-D-fructofuranosyl-(2->6)]n+1 alpha-D-glucopyranoside
-
 ?
2.4.1.10 sucrose + [beta-D-fructofuranosyl-(2->6)]n alpha-D-glucopyranoside
-
 Priestia megaterium D-glucose + [beta-D-fructofuranosyl-(2->6)]n+1 alpha-D-glucopyranoside
-
 ?
2.4.1.10 sucrose + [beta-D-fructofuranosyl-(2->6)]n alpha-D-glucopyranoside
-
 Bacillus subtilis 168 D-glucose + [beta-D-fructofuranosyl-(2->6)]n+1 alpha-D-glucopyranoside
-
 ?
2.4.1.10 sucrose + [beta-D-fructofuranosyl-(2->6)]n alpha-D-glucopyranoside
-
 Priestia megaterium DSM 319 D-glucose + [beta-D-fructofuranosyl-(2->6)]n+1 alpha-D-glucopyranoside
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.4.1.10 Lsc3
-
 Pseudomonas syringae
2.4.1.10 SacB
-
 Bacillus subtilis