1.12.99.6: hydrogenase (acceptor)

This is an abbreviated version!
For detailed information about hydrogenase (acceptor), go to the full flat file.

Word Map on EC 1.12.99.6

Reaction

H2
+
acceptor
=
reduced acceptor

Synonyms

ECH, Ech hydrogenase, EchA, EchB, EchD, EchE, EchF, endo-hydrogenase, exo-hydrogenase, F420-reducing [NiFe] hydrogenase, factor420 hydrogenase, Fe-hydrogenase, Fe-only hydrogenase, ferredoxin hydrogenase, H2 producing hydrogenase [ambiguous], H2-sensing [NiFe] hydrogenase, Hfs, Hmd, HoxEFUYH type [NiFe] hydrogenase, HoxG, HupL, HupS, hupSLW, Hya, HyaA, HyaB, Hyb, HybA, HycE, Hyd X, Hyd-1, Hyd-2, HYD1, hydA, HydA1, HydA2, HydB, hydrogen dehydrogenase, hydrogen uptake hydrogenase, hydrogen-forming methylenetetrahydromethanopterin dehydrogenase, hydrogen-lyase, hydrogen-lyase [ambiguous], hydrogen:ferredoxin oxidoreductase, hydrogen:methylviologen oxidoreductase, hydrogenase (ferredoxin), hydrogenase 1, hydrogenase 2, hydrogenase 3, hydrogenase I (bidirectional), hydrogenase II, hydrogenase II (uptake), hydrogenase-1, hydrogenase-Fe-S, hydrogenlyase [ambiguous], HyhL, HynSL, HynSL hydrogenase, Hyq, iron-sulfur-cluster-free hydrogenase, Mbh, membrane-bound [NiFe]-hydrogenase, methyl viologen-reducing hydrogenase, methylviologen hydrogenase, Ni-Fe hydrogenase, nickel-iron hydrogenase, NiFe hydrogenase, NiFe-hydrogenase, NIFeSe-hydrogenase, regulatory hydrogenase, respiratory hydrogenase, SHI, uptake hydrogenase, uptake hydrogenase [ambiguous], uptake [NiFe] hydrogenase:, uptake [NiFe]-hydrogenase, [FeFe] hydrogenase, [FeFe]-H2ase, [FeFe]-hydrogenase, [FeFe]H2ase, [Fe] hydrogenase, [Fe]-hydA, [Fe]-hydrogenase, [Ni-Fe] hydrogenase, [NiFeSe]-hydrogenase, [NiFe] hydrogenase, [NiFe]-hydrogenase, [NiFe]-hydrogenase 2, [NiFe]-hydrogenase-2, [NiFe]H2ase, [NiFe]hydrogenase

ECTree

     1 Oxidoreductases
         1.12 Acting on hydrogen as donor
             1.12.99 With unknown physiological acceptors
                1.12.99.6 hydrogenase (acceptor)

Engineering

Engineering on EC 1.12.99.6 - hydrogenase (acceptor)

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
energy production
-
use in photochemical energy conversion systems
C81S
-
theoretical 3D strucutural model. For the wild-type, the hydrogen bond of the network involving H82 and the bridging cysteines is formed with the sulfur atom of C78 whereas for the C81S mutant, it is formed with the bridging sulfur atom from C600. Calculations indicate a water molecule close to C81, which influences the IR spectra
F110L
-
18% of wild-type H2 uptake activity. The loss of activity of the mutant protein originates from reversible oxidative inactivation
I62V
-
6% of wild-type H2 uptake activity. The loss of activity of the mutant protein originates from reversible oxidative inactivation
I62V/F110L
-
mutant enzyme shows no H2 uptake activity. The loss of activity of the mutant protein originates from reversible oxidative inactivation
C81S
-
theoretical 3D strucutural model. For the wild-type, the hydrogen bond of the network involving H82 and the bridging cysteines is formed with the sulfur atom of C78 whereas for the C81S mutant, it is formed with the bridging sulfur atom from C600. Calculations indicate a water molecule close to C81, which influences the IR spectra
-
F110L
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
18% of wild-type H2 uptake activity. The loss of activity of the mutant protein originates from reversible oxidative inactivation
-
I62V
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
6% of wild-type H2 uptake activity. The loss of activity of the mutant protein originates from reversible oxidative inactivation
-
I62V/F110L
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
mutant enzyme shows no H2 uptake activity. The loss of activity of the mutant protein originates from reversible oxidative inactivation
-
E25D
-
approx. 50% of wild-type H2 uptake activity
E25Q
-
less than 0.1% of wild-type H2 uptake activity
P498A
-
100% of wild-type activity
S499A
-
100% of wild-type activity
S499C
-
75% of wild-type activity
V74C
-
moderate increase in the Michaelis constant for H2. The mutant has the same oxidation activity as the wild-type whereas its maximal H2 production rate varies by 2 orders of magnitude
V74I
-
moderate increase in the Michaelis constant for H2
V74M
-
moderate increase in the Michaelis constant for H2, The mutant has the same oxidation activity as the wild-type whereas its maximal H2 production rate varies by 2 orders of magnitude. The ratio of maximal rates for oxidation over production ranges from 2.5 for the wild-type to 200 for the V74M mutant
V78S
-
75% of wild-type activity
D202V/K492
-
variant epHycE70, has 11fold higher hydrogen production and 7fold higher hydrogen yield from formate compared to wild-type
D210N/I271F/K545R
-
variant epHycE23-2, has 8fold higher hydrogen production and 4fold higher hydrogen yield from formate compared to wild-type
E73A
-
the catalytic activity of the mutant is comparable to native enzyme
F297L/L327Q/E382K/L415M/A504T/D542N
-
variant epHycE17, has 7fold higher hydrogen production and 4fold higher hydrogen yield from formate compared to wild-type
I333F/K554d
-
variant epHycE39, has 7fold higher hydrogen production and 3fold higher hydrogen yield from formate compared to wild-type
Q32R/V112L/G245C/F409L
-
variant epHycE21, has 15fold higher hydrogen production and 6fold higher hydrogen yield from formate compared to wild-type
S2P/E4G/M314V/T366S/V394D/S397C
-
variant epHycE67, has 13fold higher hydrogen production and 5fold higher hydrogen yield from formate compared to wild-type
S2T/Y50F/I171T/A291V/T366S/V433L/M444I/L523Q
-
shows a 17fold higher hydrogen-producing activity and 8fold higher hydrogen yield from formate than wild type HycE; variant epHycE95, has 17fold higher hydrogen-producing activity and 8fold higher hydrogen yield from formate compared to wild-type
T366
-
variant satHycE12T366, has 30fold higher hydrogen production compared to wild-type; variant satHycE19T366, has 27fold higher hydrogen production compared to wild-type
Y464
-
variant shufHycE1-9, has 23fold higher hydrogen production and 9fold higher hydrogen yield from formate compared to wild-type
F297L/L327Q/E382K/L415M/A504T/D542N
-
variant epHycE17, has 7fold higher hydrogen production and 4fold higher hydrogen yield from formate compared to wild-type
-
Q32R/V112L/G245C/F409L
-
variant epHycE21, has 15fold higher hydrogen production and 6fold higher hydrogen yield from formate compared to wild-type
-
S2T/Y50F/I171T/A291V/T366S/V433L/M444I/L523Q
-
shows a 17fold higher hydrogen-producing activity and 8fold higher hydrogen yield from formate than wild type HycE; variant epHycE95, has 17fold higher hydrogen-producing activity and 8fold higher hydrogen yield from formate compared to wild-type
-
C176A
-
the Cys176 sulfur and unknown ligands of the iron complex of the wild-type enzyme are replaced by the dithiothreitol present in the crystallization solution
C250A
-
reduced activity
A204F
-
no difference in activity with 2,3-dimethyl1,4-naphthoquinone and benzyl viologen to wild-type
D100N
-
no difference in activity with 2,3-dimethyl1,4-naphthoquinone and benzyl viologen to wild-type
D88N
-
no difference in activity with 2,3-dimethyl1,4-naphthoquinone and benzyl viologen to wild-type
E94Q
-
no difference in activity with 2,3-dimethyl1,4-naphthoquinone and benzyl viologen to wild-type
G125L
-
no difference in activity with 2,3-dimethyl1,4-naphthoquinone and benzyl viologen to wild-type
H186A
-
no acitivity with 2,3-dimethyl1,4-naphthoquinone
H200A
-
no acitivity with 2,3-dimethyl1,4-naphthoquinone
H25A
-
no acitivity with 2,3-dimethyl1,4-naphthoquinone
H67A
-
no acitivity with 2,3-dimethyl1,4-naphthoquinone
M203I
-
no difference in activity with 2,3-dimethyl1,4-naphthoquinone and benzyl viologen to wild-type
N128D
-
5% of wild-type activity with 2,3-dimethyl1,4-naphthoquinone
P129A
-
no difference in activity with 2,3-dimethyl1,4-naphthoquinone and benzyl viologen to wild-type
Q131L
-
2% of wild-type activity with 2,3-dimethyl1,4-naphthoquinone
Y114F
-
no difference in activity with 2,3-dimethyl1,4-naphthoquinone and benzyl viologen to wild-type
Y127A
-
9% of wild-type activity with 2,3-dimethyl1,4-naphthoquinone
Y127F
-
no difference in activity with 2,3-dimethyl1,4-naphthoquinone and benzyl viologen to wild-type
Y127H
-
no difference in activity with 2,3-dimethyl1,4-naphthoquinone and benzyl viologen to wild-type
Y202F
-
almost no activity with 2,3-dimethyl1,4-naphthoquinone
additional information