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
-
methane-oxidizing
- methylocystis
- ch4
- methylomonas
- dioxygen
-
dinuclear
- methylobacter
- trichloroethylene
- methylomicrobium
- alkane
-
diironii
-
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
ECTree
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Purification
Purification on EC 1.14.13.25 - methane monooxygenase (soluble)
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3 components: a soluble CO-binding cytochrome c, a copper-containing protein, another small protein
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component D of sMMO recombinant from Escherichia coli as His-tagged thioredoxin-fusion protein, the thioredoxin is cleaved off during purification by factor Xa
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DEAE-Sepharose column chromatography, Q sepharose column chromatography, S-200 gel filtration, and S-300 gel filtration
native enzyme 8.08fold by anion exchange chromatography, ultrafiltration, gel filtration, and again anion exchange chromatography, to 95% purity
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native enzyme complex from cell culture by two different steps of anion exchange chromatography, recombinant subunits MMOB and MMOR from Escherichia coli strain BL21(DE3) by two different steps of anion exchange chromatography, and gel filtration, recombinant His-MBP-tagged MMOD from Escherichia coli strain Rosetta (DE3) by nickel and amylose affinity chromatography, the tag is cleaved off by tobacco etch virus protease followed by anion exchange chromatography and gel filtration
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native MMOH, in the purification procedure includes anion exchange chromatography and gel filtration
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recombinant component protein B of sMMO as glutathione-S-transferase fusion protein from Escherichia coli
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recombinant enzyme component MMOB from Escherichia coli by solubilization from the 12000 x g pellet with 8 M urea, followed by dilution for enzyme refolding, and gel filtration
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recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
A0A2D2D5X0; A0A2D2D0T8; Q53563; A0A2D2D0X7
recombinant subunits from Escherichia coli strain BL21(DE3) by two different steps of anion exchange chromatography, and gel filtration
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sMMO protein B wild-type and mutants recombinant from Escherichia coli by affinity chromatography, high salt concentration increases the binding stability between protein B and hydroxylase of sMMO
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