Literature summary for 2.4.1.10 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 .

Protein Variants

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

Localization

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

Natural Substrates/ Products (Substrates)

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

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

Substrates and Products (Substrate)

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

Synonyms	Comment	Organism
Lsc3	-	Pseudomonas syringae
SacB	-	Bacillus subtilis