1.14.13.25: methane monooxygenase (soluble)
This is an abbreviated version!
For detailed information about methane monooxygenase (soluble), go to the full flat file.
Word Map on EC 1.14.13.25
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1.14.13.25
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methanotrophs
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methanol
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methylosinus
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capsulatus
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methylococcus
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trichosporium
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methane-oxidizing
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methylocystis
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ch4
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methylomonas
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dioxygen
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dinuclear
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methylobacter
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trichloroethylene
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methylomicrobium
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alkane
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diironii
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ammonia-oxidizing
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landfill
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upland
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antiferromagnetically
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wetland
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high-valent
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non-motile
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copper-containing
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carboxylate-bridged
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peat
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copper-dependent
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dicopper
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ch3oh
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nitrosomonas
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cometabolic
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diferrous
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methanobactins
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energy production
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mixed-valent
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gammaproteobacterial
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sphagnum
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t-rflp
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seep
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propene
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synthesis
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biotechnology
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degradation
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exafs
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nitrify
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peroxo
- 1.14.13.25
- methanotrophs
- methanol
- methylosinus
- capsulatus
- methylococcus
- trichosporium
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methane-oxidizing
- methylocystis
- ch4
- methylomonas
- dioxygen
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dinuclear
- methylobacter
- trichloroethylene
- methylomicrobium
- alkane
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diironii
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ammonia-oxidizing
-
landfill
-
upland
-
antiferromagnetically
-
wetland
-
high-valent
-
non-motile
-
copper-containing
-
carboxylate-bridged
-
peat
-
copper-dependent
-
dicopper
- ch3oh
- nitrosomonas
-
cometabolic
-
diferrous
-
methanobactins
- energy production
-
mixed-valent
-
gammaproteobacterial
- sphagnum
-
t-rflp
-
seep
- propene
- synthesis
- biotechnology
- degradation
-
exafs
-
nitrify
-
peroxo
Reaction
Synonyms
chcA, cytoplasmic methane monooxygenase, methane hydroxylase, methane mono-oxygenase, methane monooxygenase, methane monooxygenase hydroxylase, MmMmoC, MMO, MMO Bath, MMOB, MmoC, MMOH, MMOR, oxygenase, methane mono-, particulate methane monooxygenase, pMMO, sMMO, soluble methane monooxygenase, soluble methane monooxygenase hydroxylase
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Engineering
Engineering on EC 1.14.13.25 - methane monooxygenase (soluble)
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G10A/G13Q/G16A
G13Q
G10A/G13Q/G16A
G13Q
A115C
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site-directed mutagenesis of enzyme component MMOH, mobility and accessibility parameters for the spin-labeled MMOB mutants alone and in complex with MMOH in comparison to the wild-type enzyme, overview
A62C
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site-directed mutagenesis of enzyme component MMOH, mobility and accessibility parameters for the spin-labeled MMOB mutants alone and in complex with MMOH in comparison to the wild-type enzyme, overview, the mutant MMOH-MMOB complex is perturbed by salts but not nonionic detergents
D71C
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site-directed mutagenesis of enzyme component MMOH, mobility and accessibility parameters for the spin-labeled MMOB mutants alone and in complex with MMOH in comparison to the wild-type enzyme, overview
D87C
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site-directed mutagenesis of enzyme component MMOH, mobility and accessibility parameters for the spin-labeled MMOB mutants alone and in complex with MMOH in comparison to the wild-type enzyme, overview
G119C
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site-directed mutagenesis of enzyme component MMOH, mobility and accessibility parameters for the spin-labeled MMOB mutants alone and in complex with MMOH in comparison to the wild-type enzyme, overview
H33A
A0A2D2D5X0; A0A2D2D0T8; Q53563; A0A2D2D0X7
site-directed mutagenesis, an N-terminal region variant, structure analysis
H5A
A0A2D2D5X0; A0A2D2D0T8; Q53563; A0A2D2D0X7
site-directed mutagenesis, an N-terminal region variant, structure analysis
K15C
K44C
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site-directed mutagenesis of enzyme component MMOH, mobility and accessibility parameters for the spin-labeled MMOB mutants alone and in complex with MMOH in comparison to the wild-type enzyme, overview
L110C
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mutant shows inverted or shifted regioselectivity with naphthalene, biphenyl, and ethylbenzene as a substrate compared to the wild type enzyme
L110G
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mutant shows inverted or shifted regioselectivity with naphthalene, biphenyl, and ethylbenzene as a substrate compared to the wild type enzyme
L110R
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mutant shows inverted or shifted regioselectivity with naphthalene, biphenyl, and ethylbenzene as a substrate compared to the wild type enzyme
L110Y
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mutant shows inverted or shifted regioselectivity with naphthalene, biphenyl and ethylbenzene as a substrate compared to the wild type enzyme
N107G/S109A/S110A/T111A
A0A2D2D5X0; A0A2D2D0T8; Q53563; A0A2D2D0X7
site-directed mutagenesis, mutations in the core region, termed the Quad variant, structure analysis
N107G/S110A
A0A2D2D5X0; A0A2D2D0T8; Q53563; A0A2D2D0X7
site-directed mutagenesis, a binary derivative of the Quad variant, termed DBL1. The DBL1 mutation in MMOB leads to a loss of the S110 hydrogen bond with N214 of the sMMOH alpha-subunit, structure analysis
R133C
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site-directed mutagenesis of enzyme component MMOH, mobility and accessibility parameters for the spin-labeled MMOB mutants alone and in complex with MMOH in comparison to the wild-type enzyme, overview
S109A/T111A
A0A2D2D5X0; A0A2D2D0T8; Q53563; A0A2D2D0X7
site-directed mutagenesis, a binary derivative of the Quad variant, termed DBL2, structure analysis
S109C
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site-directed mutagenesis of enzyme component MMOH, mobility and accessibility parameters for the spin-labeled MMOB mutants alone and in complex with MMOH in comparison to the wild-type enzyme, overview
T111C
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site-directed mutagenesis of enzyme component MMOH, mobility and accessibility parameters for the spin-labeled MMOB mutants alone and in complex with MMOH in comparison to the wild-type enzyme, overview
T111Y
V39C
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site-directed mutagenesis of enzyme component MMOH, mobility and accessibility parameters for the spin-labeled MMOB mutants alone and in complex with MMOH in comparison to the wild-type enzyme, overview
V39F
A0A2D2D5X0; A0A2D2D0T8; Q53563; A0A2D2D0X7
site-directed mutagenesis in the MMOB component, the mutant component variant nearly halts the reaction of the reconstituted sMMO system
V39R
A0A2D2D5X0; A0A2D2D0T8; Q53563; A0A2D2D0X7
site-directed mutagenesis in the MMOB component, the mutant component variant nearly halts the reaction of the reconstituted sMMO system
V41E
A0A2D2D5X0; A0A2D2D0T8; Q53563; A0A2D2D0X7
site-directed mutagenesis in the MMOB component, the mutant component variant nearly halts the reaction of the reconstituted sMMO system
V41F
A0A2D2D5X0; A0A2D2D0T8; Q53563; A0A2D2D0X7
site-directed mutagenesis in the MMOB component, the mutant component variant nearly halts the reaction of the reconstituted sMMO system
V41R
A0A2D2D5X0; A0A2D2D0T8; Q53563; A0A2D2D0X7
site-directed mutagenesis in the MMOB component, the mutant component variant nearly halts the reaction of the reconstituted sMMO system
V68C
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site-directed mutagenesis of enzyme component MMOH, mobility and accessibility parameters for the spin-labeled MMOB mutants alone and in complex with MMOH in comparison to the wild-type enzyme, overview
Y102C
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site-directed mutagenesis of enzyme component MMOH, mobility and accessibility parameters for the spin-labeled MMOB mutants alone and in complex with MMOH in comparison to the wild-type enzyme, overview
additional information
G10A/G13Q/G16A
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His-tagged protein B of sMMO, triple mutant is resistant to degradation in contrast to the wild-type, N-terminus is responsible for unusual mobility in size exclusion chromatography and proteolytic sensitivity of protein B
G13Q
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enhanced temperature stability compared to wild-type, site-directed mutagenesis
G13Q
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sMMO, alteration of a cleavage site in component protein B
G10A/G13Q/G16A
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His-tagged protein B of sMMO, triple mutant is resistant to degradation in contrast to the wild-type, N-terminus is responsible for unusual mobility in size exclusion chromatography and proteolytic sensitivity of protein B
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site-directed mutagenesis of enzyme component MMOH, mobility and accessibility parameters for the spin-labeled MMOB mutants alone and in complex with MMOH in comparison to the wild-type enzyme, overview
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mutant enzyme with increased rate constant for the reaction of large substrates such as ethane, furan, and nitrobenzene with the reactive MMOH (regulatory componant of the enzyme) intermediate Q while decreasing the rate constant for the reaction with methane. The regiospecificity for nitrobenzene oxidation is altered and 10fold more T111Y than wild-type MMOB is required to maximize the rate of turnover
T111Y
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the T111Y variant of MMOB causes only a small increase in reactivity
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native parallel occurence of full length and 2 N-terminal truncated forms of regulatory component protein B of sMMO, truncated forms are inactive
additional information
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mutagenesis of MMOB potentially broadening the substrate range of the enzyme
additional information
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substitution of MMOB or MMOR from another type II methanotroph, Methylocystis species M, retains specific enzyme activities, demonstrating the successful cross-reactivity of Methylosinus sporium strain 5
additional information
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substitution of MMOB or MMOR from another type II methanotroph, Methylocystis species M, retains specific enzyme activities, demonstrating the successful cross-reactivity of Methylosinus sporium strain 5
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additional information
Methylosinus sporium ATCC 35069
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substitution of MMOB or MMOR from another type II methanotroph, Methylocystis species M, retains specific enzyme activities, demonstrating the successful cross-reactivity of Methylosinus sporium strain 5
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additional information
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construction of deletion mutants of subunit MMOB missing 5, 8, and 13 C-terminal residues, the mutations cause progressive decreases in the maximum steady-state turnover number, as well as lower apparent rate constants for formation of the key reaction cycle intermediate compound Q, the deletions result in substantial uncoupling at or before the P intermediate due to competition between slow H2O2 release from one of the intermediates and the reaction that carries this intermediate on to the next step in the cycle, which is slowed by the mutation
additional information
A0A2D2D5X0; A0A2D2D0T8; Q53563; A0A2D2D0X7
construction of N- and C-terminal truncation variants. The dramatic effects of specific mutations on specific steps of the reaction cycle include the (i) retarding O2-binding (MMOB DELTA2-29 and V41R), (ii) uncoupling the O2-activation reaction from hydrocarbon oxidation (MMOB DELTA126-138), (iii) relaxing the size-selective entry of hydrocarbon substrates (Quad, DBL2), (iv) disrupting the quantum-tunneling nature of the HAT reaction of Q with methane (Quad), and (v) significantly increasing or decreasing the rate constants of reaction cycle steps (H33A, DBL1, DELTA126-138, H5A, V41R, and V39R). Effect of the MMOB variants on small-molecule access tunnels, overview
additional information
A0A2D2D5X0; A0A2D2D0T8; Q53563; A0A2D2D0X7
establishing of a methanotrophic co-metabolic system, built in the gcSBBR seeded by soil at a ventilation opening of coal mine in the presence of Cu2+, and seeded with sMMO in Methylosinus trichosporium OB3b and particulate methane monooxygenase (pMMO) in Methylocystis parvus in a biofilm, microbial community analyses and microbial 16S rRNA sequencing, and postulated pathway of methanotrophic co-metabolic system, overview. Six kinds of methanotrophs are detected from the seeded soil, namely, Methylocystis (0.29%), Methylocystaceae_unclassified (0.16%), Methylocystaceae_uncultured (0.04%) and Methylocaldum (0.14%), Methylococcaceae_unclassified (0.10%), Methylobacteriaceae_uncultured (0.04%), totally accounting for 0.77%
additional information
A0A2D2D5X0; A0A2D2D0T8; Q53563; A0A2D2D0X7
kinetic analysis of MMOB mutants, overview
additional information
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kinetic analysis of MMOB mutants, overview
additional information
A0A2D2D5X0; A0A2D2D0T8; Q53563; A0A2D2D0X7
the two tryptophan residues in MMOB and the single tryptophan residue in MMOR are converted to 5-fluorotryptophan (5FW) by expression in defined media containing 5-fluoroindole. In addition, the mechanistically significant N-terminal region of MMOB is 19F-labeled by reaction of the K15C variant with 3-bromo-1,1,1-trifluoroacetone (BTFA). The 5FW and BTFA modifications cause minimal structural perturbation. Resonances from the 275 kDa complexes of sMMOH with 5FW-MMOB and BTFAK15C-5FW-MMOB are readily detected at 5 microM labeled protein concentration. This approach shows directly that MMOR and MMOB competitively bind to sMMOH with similar KD values, independent of the oxidation state of the sMMOH diiron cluster