Information on EC 1.14.15.7 - choline monooxygenase

Word Map on EC 1.14.15.7
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)
Please login to have access to the AMENDA and FRENDA data

The enzyme appears in viruses and cellular organisms

top print hide
EC NUMBER
COMMENTARY hide
1.14.15.7
-
top print hide
RECOMMENDED NAME
GeneOntology No.
choline monooxygenase
top print hide
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
choline + O2 + 2 reduced ferredoxin + 2 H+ = betaine aldehyde hydrate + H2O + 2 oxidized ferredoxin
show the reaction diagram
-
-
-
-
top print hide
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
redox reaction
-
-
-
-
reduction
top print hide
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
glycine betaine biosynthesis III (plants)
-
-
Glycine, serine and threonine metabolism
-
-
top print hide
SYSTEMATIC NAME
IUBMB Comments
choline,reduced-ferredoxin:oxygen oxidoreductase
The spinach enzyme, which is located in the chloroplast, contains a Rieske-type [2Fe-2S] cluster, and probably also a mononuclear Fe centre. Requires Mg2+. Catalyses the first step of glycine betaine synthesis. In many bacteria, plants and animals, betaine is synthesized in two steps: (1) choline to betaine aldehyde and (2) betaine aldehyde to betaine. Different enzymes are involved in the first reaction. In plants, the reaction is catalysed by this enzyme whereas in animals and many bacteria it is catalysed by either membrane-bound EC 1.1.99.1 (choline dehydrogenase) or soluble EC 1.1.3.17 (choline oxidase) [7]. The enzyme involved in the second step, EC 1.2.1.8 (betaine-aldehyde dehydrogenase), appears to be the same in plants, animals and bacteria. In some bacteria, betaine is synthesized from glycine through the actions of EC 2.1.1.156 (glycine/sarcosine N-methyltransferase) and EC 2.1.1.157 (sarcosine/dimethylglycine N-methyltransferase).
top
top print hide
CAS REGISTRY NUMBER
COMMENTARY hide
118390-76-4
-
top print hide
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
amaranth, cv. RRC 1036
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
biotype S1
-
-
Manually annotated by BRENDA team
no activity in Oryza sativa
-
-
-
Manually annotated by BRENDA team
gene CMO
UniProt
Manually annotated by BRENDA team
top print hide
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
physiological function
additional information
-
the CMO upstream regulatory region reveals a number of stress response-related elements, some of which may be involved in the stress tolerance shown by this species. Salt stress is perceived differently by cells than in whole plants
top print hide
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
choline + O2 + 2 reduced ferredoxin + 2 H+
betaine aldehyde hydrate + H2O + 2 oxidized ferredoxin
show the reaction diagram
choline + O2 + reduced ferredoxin
betaine aldehyde hydrate + H2O + oxidized ferredoxin
show the reaction diagram
choline + O2 + reduced ferredoxin
betaine aldehyde hydrate + oxidized ferredoxin
show the reaction diagram
choline + O2 + reduced ferredoxin + H+
betaine aldehyde hydrate + H2O + oxidized ferredoxin
show the reaction diagram
additional information
?
-
top print hide
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
choline + O2 + 2 reduced ferredoxin + 2 H+
betaine aldehyde hydrate + H2O + 2 oxidized ferredoxin
show the reaction diagram
B5UAE1
-
-
-
?
choline + O2 + reduced ferredoxin
betaine aldehyde hydrate + H2O + oxidized ferredoxin
show the reaction diagram
choline + O2 + reduced ferredoxin + H+
betaine aldehyde hydrate + H2O + oxidized ferredoxin
show the reaction diagram
additional information
?
-
top print hide
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Fe-S center
Ferredoxin
-
iron-sulfur centre
-
-
O2
-
half-maximal rate with a O2 partial pressure of 2kPa, corresponding to an concentration of 0.025 mM
reduced ferredoxin
-
-
top print hide
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
10 mM Ca2+ can replace Mg2+
Mg2+
-
maximum activity with more than 10 mM
additional information
-
Mn2+, Cu2+ or Co2+ have no effect on activity
top print hide
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(NH4)2SO4
-
more than 50% inhibition at 25 mM
betaine
-
300 mM betaine give 50% inhibition
Chlorocholine
-
98% inhibition at 2.5 mM
diethylcholine
-
58% inhibition at 5 mM
ethylcholine
-
88% inhibition at 5 mM
N,N-dimethyldiethanolamine
-
32% inhibition at 5 mM
sulfocholine
-
65% inhibition at 2.5 mM
triethylcholine
-
43% inhibition at 5 mM
trimethylaminobutanol
-
15% inhibition at 2.5 mM
trimethylaminopropanol
-
27% inhibition at 2.5 mM
Zn2+
-
10 mM inhibits activity
top print hide
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
catalase
-
stimulation of activity by countering negative effects of H2O2 produced by ferredoxin autoxidation
-
top print hide
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.1
choline
-
reduced ferredoxin provided by NADPH/ferredoxin-NADP+ reductase or reconstituted chloroplasts
top print hide
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00003
-
in leaves of untreated plants
0.000036
-
in leaves of untreated plants
0.0001
-
in leaves of plants after salinization with 300 mM NaCl for three days
0.00012
-
in roots of untreated plants and after salinization with 100 mM NaCl for three days
0.00018
-
in leaves of plants after salinization with 100 mM NaCl for three days
0.00024
-
in leaves of plants after salinization with 400 mM NaCl for three days
0.00025
-
activity varies with leaf age
0.00048
-
in roots of plants after salinization with 400 mM NaCl for three days
0.00058
-
after salinization of plants with 200 mM NaCl for two weeks
top print hide
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.7
-
reduced ferredoxin provided by NADPH/ferredoxin-NADP+ reductase or reconstituted chloroplasts
top print hide
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
top print hide
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.2
sequence calculation
top print hide
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
colocalization with betaine aldehyde dehydrogenase
Manually annotated by BRENDA team
-
colocalization with betaine aldehyde dehydrogenase
Manually annotated by BRENDA team
additional information
top print hide
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
top print hide
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
42800
x * 42800, sequence calculation
42860
MALDI-MS after fractionation with HPLC
42880
prediction from cloned polypeptide
43000
* 43000, recombinant enzyme, SDS-PAGE
44800
x * 44800, about, sequence calculation
45000
-
SDS-PAGE
98000
-
gel filtration with Ultrogel AcA 34
133000
gel filtration with tandem Superose 12-Superdex 200
135000
native electrophoresis
top print hide
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
top print hide
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 50% glycerol, 1 month, without loss of activity
-
top print hide
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
extracts are prepared
recombinant AnCMO
top print hide
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
coexpression of chloroplast CMO and Spinacia oleracea betaine aldehyde dehydrogenase BADH genes in Lolium perenne via particle bombardment
-
DNA and amino acid sequence determination and analysis, genetic structure, most rice CMO transcripts are processed incorrectly, retaining introns or deleted of coding sequences, the unusual deletion events occurr at sequence elements of the short-direct repeats
expression analysis at normal and abiotic stress conditions, overview
-
expression in Escherichia coli
expression in Escherichia coli, Synechococcus sp. PCC7942 and Arabidopsis thaliana
expression of CMO via plastid genetic engineering in transgenic Nicotiana tabacum cv. Wisconsin 38 plants, which show accumulation of glycine betaine and increased tolerance to abiotic stress
-
gene CMO, DNA and amino acid sequence determination and analysis, phylogenetic tree, recombinant expression in transgenic Nicotiana tabacum plants via Agrobacterium tumefaciens strain LBA4404 transfection system leading to increased salt tolerance in the transgenic plants
gene HvCMO, DNA and amino acid sequence determination and analysis, phylogenetic tree, quantitative real-time PCR expression analyis, recombinant expression in Saccharomyces cerevisiae strain BJ5458
gene OsCMO, DNA and amino acid sequence determination and analysis, phylogenetic analysis, functional OsCMO expression in transgenic Nicotiana tabacum cv. Xanthinc plants using Agrobacterium tumefaciens EHA105 for transfection, overexpressing plants show increased glycine betaine content and elevated tolerance to salt stress
Gossypium hirsutum is transformed with the Atriplex hortensis CMO gene mediated by Agrobacterium tumefaciens
into a TA cloning system for sequencing
overexpression in Oryza sativa by Agrobacterium tumefaciens-mediated transformation, single copy of the transgene
-
quantitative real-time reverse transcriptase PCR expression analysis
-
top print hide
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression of CMO protein is increased by the presence of NaCl in younger leaves but decreased in older leaves
-
level of choline monooxygenase in expanded leaves increases significantly on salt stress
-
level of choline monooxygenase increases under salt stress
salt treatment results in increased expression of the enzyme mainly in the leaves but not in the roots. Thereby the expression of CMO protein is increased by the presence of NaCl in younger leaves but decreased in older leaves
-
the enzyme expression is salt- and osmotic stress-induced in seedlings, but downregulated in cell suspension culture in response to the same salt stress
-
the enzyme expression is salt- and osmotic stress-induced in seedlings, but downregulated in cell suspension culture in response to the same salt stress. CMO induction proceeds via an ABA-independent signal transduction pathway
-
the expression of HvCMO protein is increased by the presence of high NaCl, accumulation of HvCMO mRNA is increased by high osmotic and low-temperature environments
top print hide
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C181A
second Cys in the putative consensus sequence for coordination of Rieske-type cluster to Ser, Ala and Thr, essential for activity
C181S
second Cys in the putative consensus sequence for coordination of Rieske-type cluster to Ser, Ala and Thr, essential for activity
C181T
second Cys in the putative consensus sequence for coordination of Rieske-type cluster to Ser, Ala and Thr, essential for activity
H287A
first His in the putative consensus sequence for coordination of mononuclear non-heme Fe to Gly, Ala, and Val, His-287 is essential for activity
H287G
first His in the putative consensus sequence for coordination of mononuclear non-heme Fe to Gly, Ala, and Val, His-287 is essential for activity
H287V
first His in the putative consensus sequence for coordination of mononuclear non-heme Fe to Gly, Ala, and Val, His-287 is essential for activity
additional information
top print hide
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
agriculture
enhancing glycine betaine synthesis is one of the most promising ways to improve salt tolerance in cotton
top
top
top
LINKS TO OTHER DATABASES (specific for EC-Number 1.14.15.7)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
SYSTERS
Protein Mutant Database
InterPro (database of protein families, domains and functional sites)