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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

Reaction

methane
+
NAD(P)H
 +
H+
 +
O2
=
methanol
 +
NAD(P)+
 +
H2O

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

     1 Oxidoreductases
         1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
             1.14.13 With NADH or NADPH as one donor, and incorporation of one atom of oxygen into the other donor
                1.14.13.25 methane monooxygenase (soluble)

Expression

Expression on EC 1.14.13.25 - methane monooxygenase (soluble)

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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
activity of pMMO in whole cells is approximately 10fold greater than that of the purified sample
expressed in copper-limited conditions
necessary for the expression are a sigma(54)-dependent transcriptional activator, MmoR, and a putative GroEL-like chaperone, MmoG
-
sMMO is expressed at low copper/biomass ratios
sMMO is produced when the copper/biomass ratio is low
-
soluble, methane monooxygenase (sMMO) is expressed and active in the presence of copper if gold is also simultaneously present. Such expression is due to gold binding to methanobactin produced by Methylosinus trichosporium OB3b, thereby limiting copper uptake. Such expression and activity is significantly reduced if methanobactin preloaded with copper is also added. Both soluble, methane monooxygenase (sMMO) and particulate methane monooxygenase (pMMO) can be expressed when copper and gold are present, as gold effectively competes with copper for binding to methanobactin. Under certain geochemical conditions, both forms of methane monooxygenase may be expressed and active in situ
P27353; P27355; P27354; P27356; Q53563; Q53562
the enzyme is strongly regulated by the availability of copper. Methanobactin produced by Methylosinus trichosporium OB3b plays a key role in controlling expression of MMO genes in this strain. When Methylosinus trichosporium OB3b is grown in the presence of CuCl2, expression of mmoX, encoding a subunit of the hydroxylase component of sMMO, is very low. Gene mmoX expression increases, when methanobactin from Methylocystis sp. strain SB2 (SB2-Mb) is added, as does whole-cell sMMO activity, but there is no significant change in the amount of copper associated with Methylosinus trichosporium OB3b. When Methylosinus trichosporium OB3b is grown in the absence of CuCl2, the mmoX expression level is high but decreases by several orders of magnitude when copper prebound to SB2-Mb (Cu-SB2-Mb) is added, and biomass-associated copper is increased. Exposure of Methylosinus trichosporium OB3b to SB2-Mb has no effect on expression of mbnA, encoding the polypeptide precursor of methanobactin in either the presence or absence of CuCl2. Gene mbnA expression is reduced when Cu-SB2-Mb is added in both the absence and presence of CuCl2. Methanobactin acts as a general signaling molecule in methanotrophs
-
the sMMO enzyme is expressed when cells are essentially starved for copper and the copper-to-biomass ratio is low (less than 0.0002 mM Cu2+)
transcription of sMMO is arrested in cells exposed to high levels of copper ions and sMMO mRNA transcripts are not detected 15 min after the addition of CuSO4