Information on EC 4.2.1.30 - glycerol dehydratase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
4.2.1.30
-
RECOMMENDED NAME
GeneOntology No.
glycerol dehydratase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
glycerol = 3-hydroxypropanal + H2O
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
elimination
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
1,3-propanediol biosynthesis (engineered)
-
-
glycerol degradation III
-
-
Glycerolipid metabolism
-
-
SYSTEMATIC NAME
IUBMB Comments
glycerol hydro-lyase (3-hydroxypropanal-forming)
Requires a cobamide coenzyme.
CAS REGISTRY NUMBER
COMMENTARY hide
9077-68-3
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
large, middle and small subunit
A8CH84 and A8CH91 and A8CH95
UniProt
Manually annotated by BRENDA team
gene dhaB1
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
208-A
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
ATCC 33429 and ATCC 33430. Insertion of a prophage into the dehydratase-encoding region of Escherichia blattae DSM 4481 results in the loss of gene function
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
-
GDH loses most of its beta-subunit after purification by either ion exchange chromatography or using a nickel chelate column
metabolism
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1,2-ethanediol
acetaldehyde + H2O
show the reaction diagram
1,2-propandiol
propionaldehyde + H2O
show the reaction diagram
-
-
-
-
1,2-propanediol
propionaldehyde + H2O
show the reaction diagram
1,3-butanediol
? + H2O
show the reaction diagram
ethylene glycol
acetaldehyde + H2O
show the reaction diagram
glycerol
3-hydroxypropanal + H2O
show the reaction diagram
glycerol
3-hydroxypropionaldehyde + H2O
show the reaction diagram
glycerol
?
show the reaction diagram
pentane-1,2-diol
?
show the reaction diagram
propane-1,2-diol
?
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
glycerol
3-hydroxypropanal + H2O
show the reaction diagram
glycerol
3-hydroxypropionaldehyde + H2O
show the reaction diagram
-
-
-
-
?
glycerol
?
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5'-deoxyadenosylcobalamin
-
required
5,6-Dimethylbenzimidazolylcobamide
5,6-dimethylbenzimidazolylcobamide 5'-phosphate
-
i.e. DBCC, the inactive enzyme complex with hydroxocobalamin can be converted to the active holoenzyme by replacement of hydroxocobalamin with DBCC in the presence of MG2+ and SO32-
adenosylcobalamin
coenzyme B12
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Na+
-
2 M NaCl, stabilizes subunit A
SO32-
-
K2SO3, absolute requirement in the reactivation of the inactive enzyme complex with hydroxocobalamin
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(2,3-dihydroxypropyl)cobalamin
-
competes with coenzyme B12
(S)-but-3-ene-1,2-diol
-
irreversibly inactivates. Time-dependent inhibition of GDH to yield a complex that is spectroscopically (EPR) active. Presence of the 1,2-dihydroxybut-3-en-1-yl radical in the reaction, which has relatively high energy
Ag+
-
0.1 mM AgNO3, apoenzyme: 97% loss of activity, inactive enzyme complex with hydroxocobalamin: 19% loss of activity
CN-
-
KCN, pH 6.0, slowly inactivates
Cobeta-2,3-dihydroxypropyl-[1'-O-(4-tolyl)cobamide]
-
moderate inhibitor
cyanocobalamin
-
quite inhibitory to enzyme activity if it is added to the apoenzyme before the 5,6-dimethylbenzimidazolylcobamide
glycerol
Hexadecyltrimethylammonium bromide
-
0.14%, complete irreversible inactivation of the apoenzyme
Hg2+
-
0.1 mM HgCl2, apoenzyme: complete loss of activity, inactive enzyme complex with hydroxocobalamin: 70% loss of activity
HO-(CH2)n-cobalamin
-
chain lengths of n=2-5, short chains are more effective
hydroxycobalamin
-
-
Li+
-
inactivates subunit B
N-ethylmaleimide
-
1.0 mM blocks enzymatic reaction
p-chloromercuribenzoate
phenyl mercuri acetate
-
-
salicylic acid
-
causes inactivation by dissociation of the apoenzyme into its subunits
tetraethylammonium chloride
-
blocks the apoenzyme assay
vitamin B12
-
inactivated in vitro by all forms of vitamin B12 stoichiometrically
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
adenosylcobalamin
adenylcobamide
-
activates
coenzyme B12
DhaF
-
DhaG
-
GdrA
-
GdrA protein
-
recombinant GdrA and GdrB proteins form a tight complex of (GdrA)2(GdrB)2, which reactivates the glycerol- or O2-inactivated enzyme as well as the as the enzyme-cyanocobalamin complex in the presence of ATP, Mg2+ and adenosylcobalamin
-
GdrB
-
GdrB protein
-
recombinant GdrA and GdrB proteins form a tight complex of (GdrA)2(GdrB)2, which reactivates the glycerol- or O2-inactivated enzyme as well as the as the enzyme-cyanocobalamin complex in the presence of ATP, Mg2+ and adenosylcobalamin
-
glycerol dehydratase activating enzyme
-
glycerol dehydratase is activated by another enzyme termed the glycerol dehydratase activating enzyme, GD-AE, leading to formation of a glycyl radical. Formation of the glycyl radical requires a reduced iron-sulfur cluster, contained by GD-AE, and S-adenosyl-L-methionine. The GD-AE harbors adenosine and catalytic cluster (CX3CX2C) binding motifs, an additional [4Fe-4S] cluster binding motifs in the primary structure of the GD-AE and multiple Fe-S clusters that may or may not be spin-coupled
-
glycerol dehydratase reactivating factor
-
-
-
glycerol dehydratase-activating enzyme
-
activated the enzyme
-
glycerol dehydratase-reactivating factor
-
reactivating factor for diol dehydratase
-
S-adenosyl-L-methionine
-
glycerol dehydratase requires S-adenosyl-L-methionine and strictly anoxic conditions
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.07
1,2-ethanediol
pH 8.0, 37°C; pH 8.0, 37°C; pH 8.0, 37°C
0.00002 - 7
1,2-propanediol
8 - 20
adenosylcobalamin
1.08 - 1.56
ethanediol
0.4 - 3.3
glycerol
0.2 - 0.24
pentane-1,2-diol
0.25 - 0.36
Propane-1,2-diol
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
430 - 890
glycerol
200 - 310
pentane-1,2-diol
392
Propane-1,2-diol
Klebsiella pneumoniae
-
37°C, recombinant enzyme, purification method 2
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
660 - 1400
glycerol
135
840 - 1500
pentane-1,2-diol
164721
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.299
Q59475 and A6NA24 and A6NA25
recombined glycerol dehydratase
21.2
A8CH84 and A8CH91 and A8CH95
crude extract, at pH 8.5 and 45°C
65.4 - 120
-
dependent on purification method
228
-
apoenzyme
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.8 - 6
-
-
7.5
-
mutant enzymes I498S, Q42A, Q42L, Q42M, Q42T, Q42V, Q42W, Q42Y and Q42G
9
-
wild-type enzyme and mutant enzymes I498C, I498A, I498N, I498V, Q42H and Q42P
9.5
-
mutant enzymes Q42N, Q42D, Q42F, Q42K, Q42R, Q42S, Q42Y and Q42G
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 8
-
optimal enzyme activity between
7 - 9.5
A8CH84 and A8CH91 and A8CH95
the relative enzyme activity at pH values ranging from 7.0 to 9.5 is over 80%. Activity drops dramatically when the pH value is higher than 9.5
8 - 9
-
enzyme activity between
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
-
mutant enzyme I498C
42
-
mutant enzymes I498M, I498N, I498P, I498S, I498W, Q42A, Q42C, Q42D, Q42E, Q42G, Q42K, Q42L, Q42M, Q42N, Q42P, Q42T, Q42V, Q42W and Q42Y
46.7
-
mutant enzyme Q42S
47
-
mutant enzymes Q42F and Q42H
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37 - 45
assay range; assay range; assay range
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
16101
Q59475 and A6NA24 and A6NA25
x * 60702 + x * 21322 + x * 16101, alphabetagamma, sequence analysis
16121
-
alpha2,beta2,gamma2, 2 * 60433 + 2 * 21487 + 2 * 16121, calculation from sequence of amino acid
16722
-
alpha2,beta2,gamma2, 2 * 60813 + 2 * 19549 + 2 * 16722, calculation from sequence of amino acid
17700
-
x * 60700 + x * 229000 + x * 161000, alphabetagamma including His6-tag, SDS-PAGE. x * 83800 + x * 17700, GDHAB/C, SDS-PAGE. x * 85100 + x * 17700, GDHALB/C, SDS-PAGE. x * 60700 + x * 40900, GDHA/CB. x * 60700 + x * 42200, GDHA/CLB, SDS-PAGE
19549
-
alpha2,beta2,gamma2, 2 * 60813 + 2 * 19549 + 2 * 16722, calculation from sequence of amino acid
21322
Q59475 and A6NA24 and A6NA25
x * 60702 + x * 21322 + x * 16101, alphabetagamma, sequence analysis
21355
-
2! beta (alpha, gamma) 1 * 21355 (subunit A) + (1 * 60659 + 1 * 16104) (subunit B) calculation from sequence of amino acid
21487
-
alpha2,beta2,gamma2, 2 * 60433 + 2 * 21487 + 2 * 16121, calculation from sequence of amino acid
40900
-
x * 60700 + x * 229000 + x * 161000, alphabetagamma including His6-tag, SDS-PAGE. x * 83800 + x * 17700, GDHAB/C, SDS-PAGE. x * 85100 + x * 17700, GDHALB/C, SDS-PAGE. x * 60700 + x * 40900, GDHA/CB. x * 60700 + x * 42200, GDHA/CLB, SDS-PAGE
42200
-
x * 60700 + x * 229000 + x * 161000, alphabetagamma including His6-tag, SDS-PAGE. x * 83800 + x * 17700, GDHAB/C, SDS-PAGE. x * 85100 + x * 17700, GDHALB/C, SDS-PAGE. x * 60700 + x * 40900, GDHA/CB. x * 60700 + x * 42200, GDHA/CLB, SDS-PAGE
52000
-
4 * 52000, SDS-PAGE
60433
-
alpha2,beta2,gamma2, 2 * 60433 + 2 * 21487 + 2 * 16121, calculation from sequence of amino acid
60659
-
2! beta (alpha, gamma) 1 * 21355 (subunit A) + (1 * 60659 + 1 * 16104) (subunit B) calculation from sequence of amino acid
60700
-
x * 60700 + x * 229000 + x * 161000, alphabetagamma including His6-tag, SDS-PAGE. x * 83800 + x * 17700, GDHAB/C, SDS-PAGE. x * 85100 + x * 17700, GDHALB/C, SDS-PAGE. x * 60700 + x * 40900, GDHA/CB. x * 60700 + x * 42200, GDHA/CLB, SDS-PAGE
60702
Q59475 and A6NA24 and A6NA25
x * 60702 + x * 21322 + x * 16101, alphabetagamma, sequence analysis
60813
-
alpha2,beta2,gamma2, 2 * 60813 + 2 * 19549 + 2 * 16722, calculation from sequence of amino acid
62000
2 * 62000 + 2 * 22000 + 2 * 16000, SDS-PAGE
83800
-
x * 60700 + x * 229000 + x * 161000, alphabetagamma including His6-tag, SDS-PAGE. x * 83800 + x * 17700, GDHAB/C, SDS-PAGE. x * 85100 + x * 17700, GDHALB/C, SDS-PAGE. x * 60700 + x * 40900, GDHA/CB. x * 60700 + x * 42200, GDHA/CLB, SDS-PAGE
85100
-
x * 60700 + x * 229000 + x * 161000, alphabetagamma including His6-tag, SDS-PAGE. x * 83800 + x * 17700, GDHAB/C, SDS-PAGE. x * 85100 + x * 17700, GDHALB/C, SDS-PAGE. x * 60700 + x * 40900, GDHA/CB. x * 60700 + x * 42200, GDHA/CLB, SDS-PAGE
90000
-
gel filtration, in the presence of ethanolamine buffer containing 0.1 M KCl, subunit B dissociates into sub-subunits
161000
-
x * 60700 + x * 229000 + x * 161000, alphabetagamma including His6-tag, SDS-PAGE. x * 83800 + x * 17700, GDHAB/C, SDS-PAGE. x * 85100 + x * 17700, GDHALB/C, SDS-PAGE. x * 60700 + x * 40900, GDHA/CB. x * 60700 + x * 42200, GDHA/CLB, SDS-PAGE
188000
-
sucrose density gradient centrifugation, inactive enzyme complex with hydroxocobalamin
189000
190000
-
non-denaturing PAGE
198000
-
gel filtration, native enzyme
200000
220000
-
native PAGE, 2 bands: 200000 Da and 220000 Da
229000
-
x * 60700 + x * 229000 + x * 161000, alphabetagamma including His6-tag, SDS-PAGE. x * 83800 + x * 17700, GDHAB/C, SDS-PAGE. x * 85100 + x * 17700, GDHALB/C, SDS-PAGE. x * 60700 + x * 40900, GDHA/CB. x * 60700 + x * 42200, GDHA/CLB, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
heterohexamer
hexamer
tetramer
-
4 * 52000, SDS-PAGE
trimer
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
native, glycerol-bound and 1,2-propanediol-bound forms, capillary batch or hanging drop vapor diffusion method
-
complexed with cyanocobalamin an propane-1,2-diol, sandwich-drop vapor diffusion method
-
substrate-free form complexed with cobalamin and K+
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 9.5
-
inactive enzyme complex with hydroxocobalamin, quite stable between pH 5.0 to pH 9.5, below pH 5.0: inactive enzyme complex with hydroxocobalamin dissociates irreversibly, liberating hydroxocobalamin, B12OH
33819
6
-
t1/2: 1 h
704770
8 - 9
-
apoenzyme is unstable below pH 8.0 and above pH 9.0
33819
8
-
t1/2: 1 h
704770
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
30 min, potassium phosphate buffer, pH 8.6, apoenzyme is quite stable. On addition of coenzyme B12 to the incubation mixture the holoenzyme is formed
46
-
4 min, 50% destruction of the apoenzyme
50
-
subunit A: quickly inactivated at temperatures above, K+ and Na+ stabilize at high concentrations
60
-
dissociation of the inactive enzyme complex with hydroxocobalamin, if the enzyme complex is heated to over 60°C. Heating products: an active subunit B, an inactive subunit A, and a B12 derivative. K+ inhibit heat-mediated dissociation
75
-
subunit B is stabilized by K+, Na2HPO4 and K2HPO4 protect against thermal inactivation
78
-
K+ stabilizes inactive enzyme complex with hydroxocobalamin
83
-
3 min, 0.6 M KCl, inactive enzyme complex with hydroxocobalamin loses 50% of activity, K+ and Rb+ have the greatest heat-stabilizing effect
additional information
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
glycerol stabilizes the apoenzyme
-
K2SO3 stabilizes the holoenzyme
-
preservation of enzyme activity requires the presence of K+ and 1,2-propanediol
-
stabilization by substrate 1,3-butanediol
-
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
holoenzyme can be protected from oxygen by addition of 50 mM K2SO3
-
33824
under aerobic conditions of incubation holoenzyme is quite unstable and quickly undergoes spontaneous irreversible inactivation
-
33823
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, soluble enzyme is stable for at least 2 weeks
-
4°C, soluble enzyme loses 25% of activity in 3 days
-
stable after lyophilization
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
by either ion exchange chromatography or on nickel chelate column
-
by Ni-nitrilotriacetate affinity chromatography followed by gel filtration
-
homogeneity, enzyme is inactive after purification, but can be reactivated with glycerol dehydratase-activating enzyme under anaerobic conditions
-
homogeneity, recombinant enzyme, 2 different purification methods
-
immobilized metal ion affinity chromatography
-
inactive enzyme complex with hydroxocobalamin
-
Ni-nitrilotriacetate affinity chromatography followed by Sephacral S-300 gel filtration
Ni-nitrilotriacetate agarose affinity column chromatography and Sephacryl S-300 gel filtration
Ni-NTA agarose column chromatography and Sephacryl S-300 gel filtration
A8CH84 and A8CH91 and A8CH95
recombinant His-tagged GDHt 2.11fold by nickel affinity chromatography and ultrafiltration; recombinant His-tagged GDHt 2.11fold by nickel affinity chromatography and ultrafiltration; recombinant His-tagged GDHt 2.11fold by nickel affinity chromatography and ultrafiltration
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
1,3-propanediol operon of dhaB1 (encodes the vitamin B12-independent glycerol dehydratase), dhaB2 (encodes the activating factor of DhaB1) tandemly arrayed with Escherichia coli yqhD gene (encodes 1,3-propanediol oxidoreductase) under the control of a constitutive, temperature-sensitive promoter, in the vector pBV220 for heterologous expression in Escherichia coli K-12 ER2925
-
expressed in Escherichia coli JM109 cells
A8CH84 and A8CH91 and A8CH95
expressed in Escherichia coli XL10-Gold cells
expression in Escherichia coli
genes dhaBCE, recombinant expression of His6-tagged GDHt in Escherichia coli strain Bl21(DE3), optimization of IPTG inducting process for recombinant GDHt to increase specific activity and ratio of soluble form using 0.8 mM IPTG at 20°C for 3 h, method development, overview; genes dhaBCE, recombinant expression of His6-tagged GDHt in Escherichia coli strain Bl21(DE3), optimization of IPTG inducting process for recombinant GDHt to increase specific activity and ratio of soluble form using 0.8 mM IPTG at 20°C for 3 h, method development, overview; genes dhaBCE, recombinant expression of His6-tagged GDHt in Escherichia coli strain Bl21(DE3), optimization of IPTG inducting process for recombinant GDHt to increase specific activity and ratio of soluble form using 0.8 mM IPTG at 20°C for 3 h, method development, overview
gldABC encoding for wild-type and mutant GDHt amplified, PCR fragment digested with NcoI and HindIII, inserted into pSE380 linearized with the same enzymes and transforming the competent cells of Escherichia coli JM109
-
overexpressed in Escherichia coli
PCR products of gdh genes for co-expressing alpha-, beta- and gamma subunits of wild-type GDH or GDHA/CB and GDHAB/C fusion constructs inserted into pET32a vector using NdeI/HindIII sites. To minimize the effect of steric hindrance, a linker peptide inserted into the fusion partners by SacI sites, resulting two plasmids (pET32aGDHA/CLB and pET32aGDHALB/C) for expressing fusion enzyme GDHA/CLB and GDHALB/C, expressed in Escherichia coli AD494(DE3)
-
pET-28a(+)-dhaBCEE expressed in Escherichia coli BL21 (DE3)
-
plasmid pCOLADuet-1::dhaB1B2::pduP::phaC1 expressed in Escherichia coli HMS174(DE3) cells
-
plasmid PKRX-T bearing the gene of the dhaBCE double digested with EcoR I and Sac I, resulting 2.7 kb fragment containing the intact dhaBCE genes inserted into pET-28a (+) vector linearized with the same enzymes. Transformation of the ligation mixture (pET-28 (+) dhaBCE) into Escherichia coli BL21 (DE3) for overexpression
Q59475 and A6NA24 and A6NA25
two classes of glycerol dehydratase in the organism, phylogenetic analysis, overview
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
R782K
-
forms a tight protein-protein complex with glycerol dehydratase-activating enzyme
I498A
-
optimal pH and optimal temperature as the wild-type. KM for glycerol comparable to the wild-type
I498C
-
active, optimal pH as the wild-type, lower optimal temperature as the wild-type. KM for glycerol comparable to the wild-type
I498D
-
active, lower optimal pH as the wild-type, optimal temperature as the wild-type. Higher KM for glycerol as the wild-type
I498M
-
active, lower optimal pH and lower optimal temperature as the wild-type. Lower KM for glycerol as the wild-type
I498N
-
active, optimal pH as the wild-type, lower optimal temperature as the wild-type. Lower KM for glycerol as the wild-type
I498P
-
active, lower optimal pH and lower optimal temperature as the wild-type. Higher KM for glycerol as the wild-type
I498S
-
active, lower optimal pH and lower optimal temperature as the wild-type. KM for glycerol comparable to the wild-type
I498T
-
active, lower optimal pH as the wild-type, optimal temperature as the wild-type. Lower KM for glycerol as the wild-type
I498V
-
alpha subunit has half-life of 11 h in contrast to 1 h for the wild-type. Optimal pH and optimal temperature as the wild-type. KM for glycerol comparable to the wild-type
I498V/Q42L
-
alpha subunit of I498V and beta subunit of Q42L have half-life of 16 h in contrast to 1 h for the wild-type
I498W
-
active, lower optimal pH and lower optimal temperature as the wild-type. KM for glycerol comparable to the wild-type
Q42A
-
active, lower optimal pH and lower optimal temperature as the wild-type. Higher KM for glycerol as the wild-type
Q42C
-
active, lower optimal pH and lower optimal temperature as the wild-type. Higher KM for glycerol as the wild-type
Q42D
-
most affected, alpha-helix around 152 positions is totally distorted. Higher optimal pH as the wild-type, lower optimal temperature as the wild-type. Higher KM for glycerol as the wild-type
Q42E
-
active, lower optimal pH and lower optimal temperature as the wild-type. KM for glycerol comparable to the wild-type
Q42F
-
most active one, catalytic activity in beta-subunit is 8.3fold higher than the wild-type. Higher optimal pH and higher optimal temperature as the wild-type. Higher KM for glycerol as the wild-type
Q42G
-
active, lower optimal pH and lower optimal temperature as the wild-type. KM for glycerol comparable to the wild-type
Q42H
-
active, optimal pH as the wild-type, higher optimal temperature as the wild-type. KM for glycerol comparable to the wild-type
Q42I
-
active, lower optimal pH and lower optimal temperature as the wild-type. Higher KM for glycerol as the wild-type
Q42K
-
active, higher optimal pH and lower optimal temperature as the wild-type. Higher KM for glycerol as the wild-type
Q42L
-
lower optimal pH and lower optimal temperature as the wild-type. Enzyme efficiency in beta-subunit for substrate glycerol is 336fold higher than that for 1,2-propanediol. Mutation at position of the beta-subunit contributes to the increase of the thermostability as well as the pH stability of the enzyme. Lower KM for glycerol as the wild-type
Q42M
-
active, lower optimal pH and lower optimal temperature as the wild-type. Higher KM for glycerol as the wild-type
Q42N
-
most affected, alpha-helix around 152 positions is totally distorted. Higher optimal pH and lower optimal temperature as the wild-type. KM for glycerol comparable to the wild-type
Q42P
-
active, optimal pH as the wild-type, lower optimal temperature as the wild-type. Higher KM for glycerol as the wild-type
Q42R
-
most affected, alpha-helix around 152 positions is totally distorted. Higher optimal pH and lower optimal temperature as the wild-type. Lower KM for glycerol as the wild-type
Q42S
-
enzyme efficiency in beta-subunit for substrate glycerol is 80fold higher than that for 1,2-propanediol. Higher optimal pH and higher optimal temperature as the wild-type. Lower KM for glycerol as the wild-type
Q42T
-
active, lower optimal pH and lower optimal temperature as the wild-type. Higher KM for glycerol as the wild-type
Q42V
-
active, lower optimal pH and lower optimal temperature as the wild-type. Higher KM for glycerol as the wild-type
Q42W
-
active, lower optimal pH and lower optimal temperature as the wild-type. Lower KM for glycerol as the wild-type
Q42Y
-
active, lower optimal pH and lower optimal temperature as the wild-type. Higher KM for glycerol as the wild-type
I498A
-
optimal pH and optimal temperature as the wild-type. KM for glycerol comparable to the wild-type
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I498C
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active, optimal pH as the wild-type, lower optimal temperature as the wild-type. KM for glycerol comparable to the wild-type
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I498D
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active, lower optimal pH as the wild-type, optimal temperature as the wild-type. Higher KM for glycerol as the wild-type
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I498M
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active, lower optimal pH and lower optimal temperature as the wild-type. Lower KM for glycerol as the wild-type
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Q42E
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active, lower optimal pH and lower optimal temperature as the wild-type. KM for glycerol comparable to the wild-type
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
biotechnology
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development of an economical and eco-friendly biological process for the production of 1,3-propanediol by an operon harboring the dhaB1, dhaB2, and yqhD genes, from renewable resources
synthesis
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