Any feedback?
Please rate this page
(all_enzymes.php)
(0/150)

BRENDA support

5.3.1.9: glucose-6-phosphate isomerase

This is an abbreviated version!
For detailed information about glucose-6-phosphate isomerase, go to the full flat file.

Word Map on EC 5.3.1.9

Reaction

alpha-D-glucose 6-phosphate
=
beta-D-fructofuranose 6-phosphate

Synonyms

6-Phosphoglucose isomerase, AfcPGI, AMF, AMF/PGI, At4g24620, autocrine motility factor, autocrine motility factor/phosphoglucose isomerase, Cupin-PGI, D-Glucose-6-phosphate isomerase, D-glucose-6-phosphate ketol-isomerase, G6-PI, Glucose 6-phosphate isomerase, Glucose phosphate isomerase, Glucose phosphoisomerase, glucose-6-phosphate isomerase, glucose-6-phosphate isomerase, cytosolic, Glucosephosphate isomerase 2, GPI, Hexose 6-phosphate isomerase, Hexose isomerase, Hexose monophosphate isomerase, Hexose phosphate isomerase, Hexosephosphate isomerase, Isomerase, glucose phosphate, Neuroleukin, NLK, Oxoisomerase, PGI, PGI/AMF, Pgi1, PGI2, PGI3, pgiA, PHI, Phosphoglucoisomerase, Phosphoglucose isomerase, phosphoglucose isomerase/autocrine motility factor, Phosphohexoisomerase, Phosphohexomutase, Phosphohexose isomerase, Phosphosaccharomutase, SA-36, Sperm antigen-36, SwoM, TK1111, VEG54, Vegetative protein 54

ECTree

     5 Isomerases
         5.3 Intramolecular oxidoreductases
             5.3.1 Interconverting aldoses and ketoses, and related compounds
                5.3.1.9 glucose-6-phosphate isomerase

Engineering

Engineering on EC 5.3.1.9 - glucose-6-phosphate isomerase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E93A
Ni2+ content and apparent Ni2+ binding ability is reduced
E93D
catalytic efficiency is reduced by more than 100fold. Ni2+ content and apparent Ni2+ binding ability is reduced
G79A
mutant enzyme exhibits a lower thermostability, catalytic efficiency is reduced by more than 100fold
G79L
mutant enzyme exhibits a lower thermostability, catalytic efficiency is reduced by more than 100fold
H136A
catalytic efficiency remains about the same compared to wild-type activity
H80A
catalytic efficiency is reduced by more than 100fold. Ni2+ content and apparent Ni2+ binding ability is reduced
H80D
catalytic efficiency is reduced by more than 100fold. Ni2+ content and apparent Ni2+ binding ability is reduced
H82A
catalytic efficiency is reduced by more than 15fold, catalytic efficiency is reduced by more than 15fold. Ni2+ content and apparent Ni2+ binding ability is reduced
T63A
catalytic efficiency is reduced by more than 15fold
Y160F
catalytic efficiency is reduced by more than 15fold
Y95F
mutant enzyme exhibits a lower thermostability, catalytic efficiency is reduced by more than 100fold
Y95K
catalytic efficiency is reduced by more than 15fold
G189E
-
GroD1 enzyme mutant cells show 87% reduced enzyme activity and defects in glycerolipid biosynthesis, overview. The phenotype comprises profound reduction in the synthesis of phosphatidylcholine, phosphatidylethanolamine, and triglycerides but high levels of phosphatidic acid and normal levels of phosphatidylinositol synthesis, accompanied by a reduction in phosphatidate phosphatase 1 activity. Expression of wild-type hamster GPI restores GPI activity, glycerolipid biosynthesis, and PAP1 activity in GroD1
A300P
the mutation may affect the folding efficiency of the enzyme protein, the mutant shows reduced expression level and barely detectable activity
A346H
-
mutation identified in a patient suffering from chronic nonspherocytic hemolytic anemia. Loss of 82% of enzyme activity, loss of enzyme capability to dimerize. Mutation results in significant changes in erythrocyte metabolism
D511N
the mutant shows 0.44% activity compared to the wild type enzyme
E495K
E495Q
the mutant shows 0.39% activity compared to the wild type enzyme
H100L
the mutant shows 0.16% activity compared to the wild type enzyme
H389L
inactive
H389R
the mutation at or near the active site highly affects the catalytic efficiency of the enzyme, the mutant shows barely detectable activity
H396L
the mutant shows 4.2% activity compared to the wild type enzyme
I525T
K362A
inactive
L339P
L487F
the mutation decreases the enzyme tolerance to heat or SDS by mechanisms of decreasing packing efficiency
N154Q
the mutant shows 26% activity compared to the wild type enzyme
N386A
the mutant shows 36% activity compared to the wild type enzyme
Q343R
-
mutant enzymes Thr5 to Ile exhibits marked thermal instability. Mutant Thr224 to Met shows normal substrate affinity in spite of slight decrease in both specific activity and thermostability. Mutant Gln343 to Arg and Asp539 to Asn show impaired substrate affinity
Q388A
the mutant shows 5.3% activity compared to the wild type enzyme
R273H
the mutation at or near the active site highly affects the catalytic efficiency of the enzyme, the mutant shows barely detectable activity
R347C
R347H
R472H
the mutation weakens network bonding of the enzyme
R539N
-
mutant enzymes Thr5 to Ile exhibits marked thermal instability. Mutant Thr224 to Met shows normal substrate affinity in spite of slight decrease in both specific activity and thermostability. Mutant Gln343 to Arg and Asp539 to Asn show impaired substrate affinity
R75G
the mutation weakens network bonding of the enzyme
R83W
the mutation increases the water-accessible hydrophobic surface
S185A
the mutant shows 29% activity compared to the wild type enzyme
S278L
T195I
T224M
-
mutant enzymes Thr5 to Ile exhibits marked thermal instability. Mutant Thr224 to Met shows normal substrate affinity in spite of slight decrease in both specific activity and thermostability. Mutant Gln343 to Arg and Asp539 to Asn show impaired substrate affinity
T375R
the mutation decreases the enzyme tolerance to heat or SDS by mechanisms of decreasing packing efficiency
T5I
-
mutant enzymes Thr5 to Ile exhibits marked thermal instability. Mutant Thr224 to Met shows normal substrate affinity in spite of slight decrease in both specific activity and thermostability. Mutant Gln343 to Arg and Asp539 to Asn show impaired substrate affinity
V101M
the mutation decreases the enzyme tolerance to heat or SDS by mechanisms of decreasing packing efficiency
Y274F
the mutant shows 46% activity compared to the wild type enzyme
Y341F
the mutant shows 65% activity compared to the wild type enzyme
G157Y
the mutation results in a complete loss of activity
T211A
the mutant shows decreased activity with higher Km compared with that of the wild type protein
G157Y
-
the mutation results in a complete loss of activity
-
T211A
-
the mutant shows decreased activity with higher Km compared with that of the wild type protein
-
E98V
the ratio of turnover number and Km-value is 31373fold lower than that of the wild-type enzyme. The absorption maximum at 420 nm as found in wild-type enzyme is completely lost. Mutant enzyme does not contain iron or zinc or other metal
H137A
the ratio of turnover number and Km-value is 66.7fold lower than that of the wild-type enzyme. The absorption maximum at 420 nm as found in wild-type enzyme is completely lost. Mutant enzyme does not contain iron or zinc or other metal
H89A
the ratio of turnover number and Km-value is 2712fold lower than that of the wild-type enzyme. The absorption maximum at 420 nm as found in wild-type enzyme is completely lost. Mutant enzyme does not contain iron or zinc or other metal
H91A
the ratio of turnover number and Km-value is 66.7fold lower than that of the wild-type enzyme. The absorption maximum at 420 nm as found in wild-type enzyme is completely lost. Mutant enzyme does not contain iron or zinc or other metal
additional information