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Information on EC 3.5.4.9 - methenyltetrahydrofolate cyclohydrolase and Organism(s) Pseudomonas aeruginosa

for references in articles please use BRENDA:EC3.5.4.9

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IUBMB Comments

In eukaryotes, the enzyme occurs as a trifunctional enzyme that also has methylenetetrahydrofolate dehydrogenase (NADP+) (EC 1.5.1.5) and formate—tetrahydrofolate ligase (EC 6.3.4.3) activity. In some prokaryotes, it occurs as a bifunctional enzyme that also has dehydrogenase (EC 1.5.1.5) activity or formimidoyltetrahydrofolate cyclodeaminase (EC 4.3.1.4) activity.

The taxonomic range for the selected organisms is: Pseudomonas aeruginosa
The enzyme appears in selected viruses and cellular organisms

Synonyms
mthfd2, cyclohydrolase, methenyltetrahydrofolate cyclohydrolase, 5,10-methenyltetrahydrofolate cyclohydrolase, mthfd2l, 5,10-methenyl-thf cyclohydrolase, nad-dependent methylenetetrahydrofolate dehydrogenase-cyclohydrolase, methylenetetrahydrofolate dehydrogenase/cyclohydrolase, dhch1, methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase, more

SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5,10-methenyl-H4folate cyclohydrolase
-
-
-
-
Citrovorum factor cyclodehydrase
-
-
-
-
cyclohydrolase
-
-
-
-
formyl-methenyl-methylenetetrahydrofolate synthetase (combined)
-
-
-
-
methenyl-THF cyclohydrolase
-
-
-
-
N5,N10-methylenetetrahydrofolate dehydrogenase-cyclohydrolase
bifunctional enzyme
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
amidine hydrolysis
-
-
-
-
PATHWAY SOURCE
PATHWAYS
MetaCyc
folate transformations I, folate transformations II (plants), folate transformations III (E. coli), formaldehyde oxidation VII (THF pathway), formate assimilation into 5,10-methylenetetrahydrofolate, L-histidine degradation III, purine nucleobases degradation I (anaerobic), purine nucleobases degradation II (anaerobic), reductive acetyl coenzyme A pathway I (homoacetogenic bacteria), reductive glycine pathway of autotrophic CO2 fixation, tetrahydrofolate salvage from 5,10-methenyltetrahydrofolate
SYSTEMATIC NAME
IUBMB Comments
5,10-methenyltetrahydrofolate 5-hydrolase (decyclizing)
In eukaryotes, the enzyme occurs as a trifunctional enzyme that also has methylenetetrahydrofolate dehydrogenase (NADP+) (EC 1.5.1.5) and formate---tetrahydrofolate ligase (EC 6.3.4.3) activity. In some prokaryotes, it occurs as a bifunctional enzyme that also has dehydrogenase (EC 1.5.1.5) activity or formimidoyltetrahydrofolate cyclodeaminase (EC 4.3.1.4) activity.
CAS REGISTRY NUMBER
COMMENTARY hide
9027-97-8
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY hide
Reversibility
r=reversible
ir=irreversible
?=not specified
5,10-methenyltetrahydrofolate + H2O
10-formyltetrahydrofolate
show the reaction diagram
Substrates: -
Products: -
r
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY hide
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
5,10-methenyltetrahydrofolate + H2O
10-formyltetrahydrofolate
show the reaction diagram
Substrates: -
Products: -
r
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-[(2-chloro-6-fluorobenzyl)sulfanyl]-6-(trifluoromethyl)pyrimidin-4-ol
-
5-[(4-chlorophenyl)sulfonyl]-6-ethoxypyrimidine-2,4-diamine
-
6-benzyl-5-methyl-7-oxo-4,7-dihydropyrazolo[1,5-a]pyrimidine-3-carbonitrile
-
LY354899
i.e. 5,6,7,8-tetrahydro-N5,N10-carbonylfolic acid
LY374571
i.e. (2R)-2-[(4-{[(2,5-diamino-6-hydroxypyrimidin-4-yl)carbamoyl]amino}phenyl)formamido]pentanedioic acid
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.026
5,10-methenyltetrahydrofolate
at pH 7.9 and 22°C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0025
2-[(2-chloro-6-fluorobenzyl)sulfanyl]-6-(trifluoromethyl)pyrimidin-4-ol
Pseudomonas aeruginosa
at pH 7.9 and 22°C
0.0009
5-[(4-chlorophenyl)sulfonyl]-6-ethoxypyrimidine-2,4-diamine
Pseudomonas aeruginosa
at pH 7.9 and 22°C
0.0038
6-benzyl-5-methyl-7-oxo-4,7-dihydropyrazolo[1,5-a]pyrimidine-3-carbonitrile
Pseudomonas aeruginosa
at pH 7.9 and 22°C
0.00003
LY374571
Pseudomonas aeruginosa
at pH 7.9 and 22°C
top print hide Go to Organism Search
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Highest Expressing Human Cell Lines
Cell Line Links Gene Links
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
A0A071LH88_PSEAI
284
0
30549
TrEMBL
Secretory Pathway (Reliability: 1)
A0A3A2CPG3_PSEAI
284
0
30553
TrEMBL
-
A0ABD7JZW0_PSEAI
306
0
32276
TrEMBL
-
A0ABD7K0I4_PSEAI
284
0
30519
TrEMBL
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30000
2 * 30000, SDS-PAGE
60000
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
2 * 30000, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using 25% (w/v) PEG 3350 and 0.2 M magnesium formate
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni2+-charged HisTrap column chromatography and Superdex 200 gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Eadsforth, T.C.; Gardiner, M.; Maluf, F.V.; McElroy, S.; James, D.; Frearson, J.; Gray, D.; Hunter, W.N.
Assessment of Pseudomonas aeruginosa N5,N10-methylenetetrahydrofolate dehydrogenase-cyclohydrolase as a potential antibacterial drug target
PLoS ONE
7
e35973
2012
Pseudomonas aeruginosa (Q9I2U6), Pseudomonas aeruginosa
Manually annotated by BRENDA team