Information on EC 5.3.1.25 - L-Fucose isomerase

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The expected taxonomic range for this enzyme is: Bacteria

EC NUMBER
COMMENTARY
5.3.1.25
-
RECOMMENDED NAME
GeneOntology No.
L-Fucose isomerase
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-fucopyranose = L-fuculose
show the reaction diagram
-
-
-
-
L-fucopyranose = L-fuculose
show the reaction diagram
protein environment suggests strongly that the reaction belongs to the ene-diol type
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
isomerization
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
fucose degradation
-
-
degradation of hexoses
-
-
Fructose and mannose metabolism
-
-
Microbial metabolism in diverse environments
-
-
SYSTEMATIC NAME
IUBMB Comments
L-fucose aldose-ketose-isomerase
Requires a divalent metal ion (the enzyme from the bacterium Escherichia coli prefers Mn2+). The enzyme binds the closed form of the sugar and catalyses ring opening to generate a form of open-chain conformation that facilitates the isomerization reaction, which proceeds via an ene-diol mechanism [3]. The enzyme from Escherichia coli can also convert D-arabinose to D-ribulose [1]. The enzyme from the thermophilic bacterium Caldicellulosiruptor saccharolyticus also converts D-altrose to D-psicose and L-galactose to L-tagatose [4].
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D-Arabinose (L-Fucose) isomerase
-
-
-
-
D-Arabinose isomerase
-
-
-
-
EC 5.3.1.3
-
-
related
-
Fucose isomerase
-
-
-
-
Isomerase, L-fucose
-
-
-
-
L-Fucose isomerase
D-arabinose isomerase, bifunctional enzyme
L-Fucose isomerase
D-arabinose isomerase, bifunctional enzyme
L-fucose ketol-isomerase
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
60063-83-4
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Dictyoglomus turgidum DSMZ 6724
-
UniProt
Manually annotated by BRENDA team
strain B/r; strain K-12
-
-
Manually annotated by BRENDA team
strain K-12; wild type and mutant strains which constitutively synthesize the enzyme
-
-
Manually annotated by BRENDA team
Escherichia coli B/r
strain B/r
-
-
Manually annotated by BRENDA team
mutants which are capable of utilizing D-arabinose as a sole source of carbon and energy for growth
-
-
Manually annotated by BRENDA team
strain PRL-R3
-
-
Manually annotated by BRENDA team
strain W70, wild type enzyme and constitutive mutants
-
-
Manually annotated by BRENDA team
wild type strain PRL-R3 and two constitutive mutants, 502 and 510
-
-
Manually annotated by BRENDA team
Klebsiella pneumoniae M-7
strain M-7
-
-
Manually annotated by BRENDA team
Klebsiella pneumoniae PRL-R3
strain PRL-R3
-
-
Manually annotated by BRENDA team
Klebsiella pneumoniae W70
strain W70, wild type enzyme and constitutive mutants
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
D-altrose
D-psicose
show the reaction diagram
Dictyoglomus turgidum, Dictyoglomus turgidum DSMZ 6724
-
-
?
D-Arabinose
D-Ribulose
show the reaction diagram
-
-
-
-
D-Arabinose
D-Ribulose
show the reaction diagram
-
-
-
-
D-Arabinose
D-Ribulose
show the reaction diagram
-
-
-
-
D-Arabinose
D-Ribulose
show the reaction diagram
-
-
-
-
D-Arabinose
D-Ribulose
show the reaction diagram
-
-
-
-
D-Arabinose
D-Ribulose
show the reaction diagram
-
-
-
-
D-Arabinose
D-Ribulose
show the reaction diagram
-
-
-
-
D-Arabinose
D-Ribulose
show the reaction diagram
Escherichia coli B/r
-
-
-
-
D-Arabinose
D-Ribulose
show the reaction diagram
Klebsiella pneumoniae PRL-R3
-
-
-
-
D-Arabinose
?
show the reaction diagram
-
L-fuculose 1-phosphate is the inducer
-
-
-
D-Arabinose
?
show the reaction diagram
-
the enzyme catalyzes the first reaction in the degradation of D-arabinose
-
-
-
D-Arabinose
?
show the reaction diagram
-
deficiency of the enzyme results in loss of activity to utilize D-arabinose
-
-
-
D-arabinose
D-ribose
show the reaction diagram
Dictyoglomus turgidum, Dictyoglomus turgidum DSMZ 6724
-
-
?
L-Fucose
L-Fuculose
show the reaction diagram
-
-
-
-
L-Fucose
L-Fuculose
show the reaction diagram
-
-
-
-
L-Fucose
L-Fuculose
show the reaction diagram
-
-
-
-
L-Fucose
L-Fuculose
show the reaction diagram
-
-
-
-
L-Fucose
L-Fuculose
show the reaction diagram
-
-
-
-
L-Fucose
L-Fuculose
show the reaction diagram
-
-
-
-
L-Fucose
L-Fuculose
show the reaction diagram
-
-
?
L-Fucose
L-Fuculose
show the reaction diagram
highest activity
-
?
L-Fucose
L-Fuculose
show the reaction diagram
Klebsiella pneumoniae M-7
-
-
-
-
L-Fucose
L-Fuculose
show the reaction diagram
Dictyoglomus turgidum DSMZ 6724
highest activity
-
?
L-Fucose
L-Fuculose
show the reaction diagram
Escherichia coli B/r
-
-
-
-
L-Fucose
L-Fuculose
show the reaction diagram
Klebsiella pneumoniae PRL-R3
-
-
-
-
L-Fucose
L-Fuculose
show the reaction diagram
Escherichia coli K12
-
-
-
-
L-Fucose
L-Fuculose
show the reaction diagram
Klebsiella pneumoniae W70
-
-
-
-
L-Fucose
?
show the reaction diagram
-
enzyme of the metabolic pathway of L-fucose
-
-
-
L-Fucose
?
show the reaction diagram
-
L-fucose catabolic enzyme
-
-
-
L-Fucose
?
show the reaction diagram
Escherichia coli K12
-
enzyme of the metabolic pathway of L-fucose
-
-
-
L-Fucose
?
show the reaction diagram
Klebsiella pneumoniae W70
-
L-fucose catabolic enzyme
-
-
-
L-galactose
L-tagatose
show the reaction diagram
Dictyoglomus turgidum, Dictyoglomus turgidum DSMZ 6724
-
-
?
L-Xylose
L-Xylulose
show the reaction diagram
Klebsiella pneumoniae, Klebsiella pneumoniae PRL-R3
-
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
D-altrose
D-psicose
show the reaction diagram
Dictyoglomus turgidum, Dictyoglomus turgidum DSMZ 6724
B8E1T1
-
-
?
D-Arabinose
?
show the reaction diagram
-
L-fuculose 1-phosphate is the inducer
-
-
-
D-Arabinose
?
show the reaction diagram
-
the enzyme catalyzes the first reaction in the degradation of D-arabinose
-
-
-
D-Arabinose
?
show the reaction diagram
-
deficiency of the enzyme results in loss of activity to utilize D-arabinose
-
-
-
D-arabinose
D-ribose
show the reaction diagram
Dictyoglomus turgidum, Dictyoglomus turgidum DSMZ 6724
B8E1T1
-
-
?
L-Fucose
L-Fuculose
show the reaction diagram
A4XJ56
-
-
?
L-Fucose
L-Fuculose
show the reaction diagram
C0SSE7
-
-
?
L-Fucose
L-Fuculose
show the reaction diagram
B8E1T1
highest activity
-
?
L-Fucose
?
show the reaction diagram
-
enzyme of the metabolic pathway of L-fucose
-
-
-
L-Fucose
?
show the reaction diagram
-
L-fucose catabolic enzyme
-
-
-
L-Fucose
L-Fuculose
show the reaction diagram
Dictyoglomus turgidum DSMZ 6724
B8E1T1
highest activity
-
?
L-Fucose
?
show the reaction diagram
Escherichia coli K12
-
enzyme of the metabolic pathway of L-fucose
-
-
-
L-Fucose
?
show the reaction diagram
Klebsiella pneumoniae W70
-
L-fucose catabolic enzyme
-
-
-
L-galactose
L-tagatose
show the reaction diagram
Dictyoglomus turgidum, Dictyoglomus turgidum DSMZ 6724
B8E1T1
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
-
stimulates
Co2+
about 5fold stimulation of activity at 1 mM
Mg2+
about 2fold stimulation of activity at 1 mM
Mn2+
-
stimulates
Mn2+
-
required
Zn2+
about 3fold stimulation of activity at 1 mM
Mn2+
required for maximum activity (more than 10fold stimulation of activity at 1 mM), the enzyme contains one atom per monomer
additional information
Mg2+ and Ca2+ show no crucial effect on the enzyme activity
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-amino-2-methyl-1,3-propanediol
-
-
Cu2+
inhibitory at 1 mM
dithioerythritol
-
-
dithiothreitol
-
competitive
Dulcitol
-
-
EDTA
-
plus L-His
EDTA
complete inhibition at 1 mM
Fe2+
inhibitory at 1 mM
His
-
L-His: activates in presence of Mn2+, strong noncompetitive inhibition without metal ion or in presence of Mg2+, Sr2+, Ca2+, Na+ or K+. D-His has almost the same effect as L-His
L-arabitol
-
-
L-arabitol
-
-
ribitol
-
-
sorbitol
-
-
tert-Butylamine
-
weak
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
98
D-arabinose
-
constitutive mutant 531
140
D-arabinose
-
wild type strain PRL-R3
160
D-arabinose
-
constitutive mutant 502
160
D-arabinose
-
D-arabinose
170
D-arabinose
-
E. coli B/r
220
D-arabinose
-
-
280
D-arabinose
-
E. coli K-12
35
L-fucose
-
constitutive mutant 531
42
L-fucose
-
E. coli B/r
45
L-fucose
-
E. coli K-12
50
L-fucose
-
constitutive mutant 502
51
L-fucose
-
-
52
L-fucose
mutant enzyme H539A, at pH 7.0 and 80C
55
L-fucose
-
wild type strain PRL-R3
72
L-fucose
wild type enzyme, at pH 7.0 and 80C
77
L-fucose
mutant enzyme W102A, at pH 7.0 and 80C
85
L-fucose
mutant enzyme R30A, at pH 7.0 and 80C
86
L-fucose
mutant enzyme F452A, at pH 7.0 and 80C
90
L-fucose
mutant enzyme W510A, at pH 7.0 and 80C
92
L-fucose
mutant enzyme N404A, at pH 7.0 and 80C
140
L-fucose
mutant enzyme D373A, at pH 7.0 and 80C
148
L-fucose
mutant enzyme V131A, at pH 7.0 and 80C
166
L-fucose
mutant enzyme M197A, at pH 7.0 and 80C
202
L-fucose
mutant enzyme I199A, at pH 7.0 and 80C
225
L-fucose
mutant enzyme Q314A, at pH 7.0 and 80C
302
L-fucose
mutant enzyme Y451A, at pH 7.0 and 80C
339
L-fucose
mutant enzyme N538A, at pH 7.0 and 80C
385
L-fucose
mutant enzyme S405A, at pH 7.0 and 80C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.1985
L-fucose
Caldicellulosiruptor saccharolyticus
A4XJ56
-
2.58
L-fucose
Dictyoglomus turgidum
B8E1T1
mutant enzyme W510A, at pH 7.0 and 80C
3.37
L-fucose
Dictyoglomus turgidum
B8E1T1
mutant enzyme H539A, at pH 7.0 and 80C
7.38
L-fucose
Dictyoglomus turgidum
B8E1T1
mutant enzyme Q314A, at pH 7.0 and 80C
8
L-fucose
Dictyoglomus turgidum
B8E1T1
mutant enzyme D373A, at pH 7.0 and 80C
10.37
L-fucose
Dictyoglomus turgidum
B8E1T1
mutant enzyme N404A, at pH 7.0 and 80C
17.83
L-fucose
Dictyoglomus turgidum
B8E1T1
mutant enzyme M197A, at pH 7.0 and 80C
19.17
L-fucose
Dictyoglomus turgidum
B8E1T1
mutant enzyme W102A, at pH 7.0 and 80C
20.33
L-fucose
Dictyoglomus turgidum
B8E1T1
mutant enzyme F452A, at pH 7.0 and 80C
33.33
L-fucose
Dictyoglomus turgidum
B8E1T1
mutant enzyme I199A, at pH 7.0 and 80C
41
L-fucose
Dictyoglomus turgidum
B8E1T1
mutant enzyme Y451A, at pH 7.0 and 80C
53.83
L-fucose
Dictyoglomus turgidum
B8E1T1
mutant enzyme R30A, at pH 7.0 and 80C
114.8
L-fucose
Dictyoglomus turgidum
B8E1T1
mutant enzyme N538A, at pH 7.0 and 80C
216.7
L-fucose
Dictyoglomus turgidum
B8E1T1
mutant enzyme V131A, at pH 7.0 and 80C
235
L-fucose
Dictyoglomus turgidum
B8E1T1
mutant enzyme S405A, at pH 7.0 and 80C
258.3
L-fucose
Dictyoglomus turgidum
B8E1T1
wild type enzyme, at pH 7.0 and 80C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.03
L-fucose
Dictyoglomus turgidum
B8E1T1
mutant enzyme Q314A, at pH 7.0 and 80C; mutant enzyme W510A, at pH 7.0 and 80C
717
0.06
L-fucose
Dictyoglomus turgidum
B8E1T1
mutant enzyme D373A, at pH 7.0 and 80C
717
0.07
L-fucose
Dictyoglomus turgidum
B8E1T1
mutant enzyme H539A, at pH 7.0 and 80C
717
0.11
L-fucose
Dictyoglomus turgidum
B8E1T1
mutant enzyme M197A, at pH 7.0 and 80C; mutant enzyme N404A, at pH 7.0 and 80C
717
0.14
L-fucose
Dictyoglomus turgidum
B8E1T1
mutant enzyme Y451A, at pH 7.0 and 80C
717
0.16
L-fucose
Dictyoglomus turgidum
B8E1T1
mutant enzyme I199A, at pH 7.0 and 80C
717
0.23
L-fucose
Dictyoglomus turgidum
B8E1T1
mutant enzyme F452A, at pH 7.0 and 80C
717
0.25
L-fucose
Dictyoglomus turgidum
B8E1T1
mutant enzyme W102A, at pH 7.0 and 80C
717
0.33
L-fucose
Dictyoglomus turgidum
B8E1T1
mutant enzyme N538A, at pH 7.0 and 80C
717
0.62
L-fucose
Dictyoglomus turgidum
B8E1T1
mutant enzyme R30A, at pH 7.0 and 80C; mutant enzyme S405A, at pH 7.0 and 80C
717
1.48
L-fucose
Dictyoglomus turgidum
B8E1T1
mutant enzyme V131A, at pH 7.0 and 80C
717
3.58
L-fucose
Dictyoglomus turgidum
B8E1T1
wild type enzyme, at pH 7.0 and 80C
717
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.35
mutant enzyme W510A, using L-fucose as substrate, at pH 7.0 and 80C
0.47
mutant enzyme D373A, using L-fucose as substrate, at pH 7.0 and 80C
0.67
mutant enzyme Y451A, using L-fucose as substrate, at pH 7.0 and 80C
0.93
mutant enzyme Q314A, using L-fucose as substrate, at pH 7.0 and 80C
1.3
mutant enzyme N404A, using L-fucose as substrate, at pH 7.0 and 80C
1.4
purification step crude extract, substrate L-fucose
2.1
mutant enzyme H539A, using L-fucose as substrate, at pH 7.0 and 80C
2.4
mutant enzyme M197A, using L-fucose as substrate, at pH 7.0 and 80C
2.5
mutant enzyme W102A, using L-fucose as substrate, at pH 7.0 and 80C
2.6
mutant enzyme F452A, using L-fucose as substrate, at pH 7.0 and 80C
3.4
mutant enzyme R30A, using L-fucose as substrate, at pH 7.0 and 80C
4.3
mutant enzyme I199A, using L-fucose as substrate, at pH 7.0 and 80C
6.8
mutant enzyme N538A, using L-fucose as substrate, at pH 7.0 and 80C
10
purification step heat treatment, substrate L-fucose
25.1
-
D-arabinose, constitutive mutant 502
27
mutant enzyme V131A, using L-fucose as substrate, at pH 7.0 and 80C
30
mutant enzyme S405A, using L-fucose as substrate, at pH 7.0 and 80C
33
wild type enzyme, using L-fucose as substrate, at pH 7.0 and 80C
43.5
-
L-fucose, constitutuve mutant 502
63.3
-
Escherichia coli K-12
63.7
-
Escherichia coli B/r
76
purification step His-Trap column, substrate L-fucose
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8 - 10
-
-
9.3
-
D-arabinose; L-fucose
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 8.5
about 80% activity at pH 6.5, 100% activity at pH 7.0, about 80% activity at pH 7.5, about 60% activity at pH 8.0, about 50% activity at pH 8.5
7 - 10
-
7.0: sharp decrease in activity below, 8.0-10.0: maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
65 - 90
about 50% activity at 65C, about 60% activity at 70C, about 75% activity at 75C, 100% activity at 80C, about 75% activity at 85C, about 60% activity at 90C
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
L-fucose induced culture of strain K-12 and D-arabinose-induced culture of strain B/r
Manually annotated by BRENDA team
Escherichia coli B/r
-
L-fucose induced culture of strain K-12 and D-arabinose-induced culture of strain B/r
-
Manually annotated by BRENDA team
Klebsiella pneumoniae M-7
-
-
-
Manually annotated by BRENDA team
Escherichia coli B/r
-
strain B/r
-
Manually annotated by BRENDA team
Escherichia coli B/r
-
strain K-12
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
68000
determined by SDS-PAGE
702836
68110
theoretical
702836
204000
homotrimer, determined by gel filtration
702836
250000
-
gel filtration
2685, 2686
342000
-
strain B/r, high-speed equilibrium sedimentation
2684
355000
-
strain K-12, high-speed equilibrium sedimentation
2684
390000
-
-
2691
410000
gel filtration
727104
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexamer
-
6 * 64976, crystallographic data
homohexamer
6 * 68000, His6-tagged enzyme, SDS-PAGE; 6 * 68363, His6-tagged enzyme, calculated from amino acid sequence
homohexamer
Dictyoglomus turgidum DSMZ 6724
-
6 * 68000, His6-tagged enzyme, SDS-PAGE; 6 * 68363, His6-tagged enzyme, calculated from amino acid sequence
-
tetramer
-
4 * 84600, Escherichia coli B/r, high speed sedimentation of enzyme dissociated into subunits by protonation at pH 2 or dialysis against buffer containing 8 M urea; 4 * 90900, Escherichia coli K-12, high speed sedimentation of enzyme dissociated into subunits by protonation at pH 2 or dialysis against buffer containing 8 M urea
tetramer
Escherichia coli B/r
-
4 * 84600, Escherichia coli B/r, high speed sedimentation of enzyme dissociated into subunits by protonation at pH 2 or dialysis against buffer containing 8 M urea; 4 * 90900, Escherichia coli K-12, high speed sedimentation of enzyme dissociated into subunits by protonation at pH 2 or dialysis against buffer containing 8 M urea
-
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
three X-ray structures of D-arabinose isomerase in complexes with 2-methyl-2,4-pentadiol, glycerol and L-fucitol are determined at resolutions of 1.77, 1.60 and 2.60 A, respectively
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
55
-
about 40% loss of activity after 10 min without dithiothreitol, stable in presence of dithiothreitol
2680
80
the enzyme has half-lives of 20, 12, 7, 5, and 2 h at 65, 70,75, 80, and 85C, respectively
727104
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
dithiothreitol protects from thermal inactivation at 55 C
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
2C, crystalline enzyme is stable as a sediment in polyethylene glycol solution for at least 1 month
-
stable for more than 1 month in 50 mM Tris-HCl buffer at pH 7.5 containing 1 mM MnCl2 and mercaptoethanol
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
using an anion-exchange column, Q Sepharose high performance, a hydrophobic interaction column, RESOURCE PHE, and an anion-exchange column, RESOURCE Q
heat treatment and His-Trap affinity chromatography
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
for over-expression in Escherichia coli JM109 cells
into the vector pGEM-T Easy, and subsequently into the vector pET15b for expression in Escherichia coli ER2566 cells
expressed in Escherichia coli ER2566 cells
nucleotide sequence of the gene fucI
-
organization of the fuc regulon specifying L-fucose dissimilation as determined by gene cloning
-
overexpression in Escherichia coli
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D373A
the mutation results in a substantial increase in Km value
F452A
the mutation results in decreases in kcat, but has little effect on Km value
I199A
the mutation results in a substantial increase in Km value
M197A
the mutation results in a substantial increase in Km value
N404A
the mutation results in decreases in kcat, but has little effect on Km value
N538A
the mutation results in a substantial increase in Km value
Q314A
the mutation results in a substantial increase in Km value
R30A
the mutation results in decreases in kcat, but has little effect on Km value
S405A
the mutation results in a substantial increase in Km value
V131A
the mutation results in a substantial increase in Km value
W102A
the mutation results in decreases in kcat, but has little effect on Km value
W510A
the mutation results in decreases in kcat, but has little effect on Km value
Y451A
the mutation results in a substantial increase in Km value
D349A
Dictyoglomus turgidum DSMZ 6724
-
inactive
-
D373A
Dictyoglomus turgidum DSMZ 6724
-
the mutation results in a substantial increase in Km value
-
M197A
Dictyoglomus turgidum DSMZ 6724
-
the mutation results in a substantial increase in Km value
-
R30A
Dictyoglomus turgidum DSMZ 6724
-
the mutation results in decreases in kcat, but has little effect on Km value
-
W510A
Dictyoglomus turgidum DSMZ 6724
-
the mutation results in decreases in kcat, but has little effect on Km value
-