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
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landfill
-
upland
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antiferromagnetically
-
wetland
-
high-valent
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non-motile
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copper-containing
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carboxylate-bridged
-
peat
-
copper-dependent
-
dicopper
- ch3oh
- nitrosomonas
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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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Inhibitors
Inhibitors on EC 1.14.13.25 - methane monooxygenase (soluble)
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protein MMOB
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inhibition of sMMO auxiliary proteins MMOB or MMOD severely diminishes electron-transfer throughput from MMOR, primarily by shifting the bulk of electron transfer to the slowest pathway, the biphasic reactions for electron transfer to MMOH from several MMOR ferredoxin analogues are also inhibited, overview
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protein MMOD
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inhibition of sMMO auxiliary proteins MMOB or MMOD severely diminishes electron-transfer throughput from MMOR, primarily by shifting the bulk of electron transfer to the slowest pathway, the biphasic reactions for electron transfer to MMOH from several MMOR ferredoxin analogues are also inhibited, overview
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2,4-Dichloro-(6-phenylphenoxy)ethylamine hydrochloride
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no inhibition
Allylthiourea
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pMMO inhibitor and copper chelator. Without allylthiourea strain OB3b quickly loses sMMO activity whenever it is grown on NMS medium with methane as the sole carbon and energy source. No loss of sMMO activity when the growth substrate is switched from methane to methanol when allylthiourea is added to growth medium containing copper
Cu2+
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copper ions irreversibly inhibit the activity of sMMO in vivo and in vitro by inactivating the reductase component
Cu2+
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copper ions irreversibly inhibit the activity of sMMO in vivo and in vitro by inactivating the reductase component
Cu2+
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copper ions irreversibly inhibit the activity of sMMO in vivo and in vitro by inactivating the reductase component
Cu2+
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loss of sMMO activity with copper addition to a culture growing on methanol. Recovery of sMMO activity by addition of allylthiourea
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activation of dioxygen occurs at a diiron centre within the hydroxylase subunit. The monooxygenation of a substrate by sMMO requires only two oxidation equivalents, and, consequently, after the oxygenation the two iron centres remain in the oxidation state +III
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MMO activity dramatically decreases when cellular poly-beta-hydroxybutyrate accumulates in the second stage. The more poly-beta-hydroxybutyrate are accumulated, the slower MMO activity decreases. Cellular poly-beta-hydroxybutyrate content has some influence on the maintenance of the MMO activity
poly-beta-hydroxybutyrate
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MMO activity dramatically decreases when cellular poly-beta-hydroxybutyrate accumulates in the second stage. The more poly-beta-hydroxybutyrate are accumulated, the slower MMO activity decreases. Cellular poly-beta-hydroxybutyrate content has some influence on the maintenance of the MMO activity
poly-beta-hydroxybutyrate
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MMO activity dramatically decreases when cellular poly-beta-hydroxybutyrate accumulates in the second stage. The more poly-beta-hydroxybutyrate are accumulated, the slower MMO activity decreases. Cellular poly-beta-hydroxybutyrate content has some influence on the maintenance of the MMO activity
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sMMO is completely inhibited by monomeric component D, but not by dimeric, monomeric MMOD is interfering with the catalytically active complex between component A hydroxylase and component protein B
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additional information
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when cultivated in nutrients deficiency culture, activity of sMMO does not decrease
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additional information
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when cultivated in nutrients deficiency culture, activity of sMMO decreases
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additional information
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other possible inhibitory enzymes, such as MMOD (orfY), can inhibit its activity in the soluble portion of cell lysates
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additional information
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inhibitory role of subunit MMOD. MMOD binding leads to steric hindrance with the N-terminal region of MMOHbeta, which then triggers the detachment of MMOHbeta-NT from MMOHalpha
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additional information
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different chlorinated hydrocarbons cause different inhibition patterns
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additional information
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when cultivated in nutrients deficiency culture, activity of sMMO in strain OB3b decreases, whereas activity of sMMO in strain IMV3011 does not decrease
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