Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 1.5.1.15 - methylenetetrahydrofolate dehydrogenase (NAD+) and Organism(s) Methanosarcina barkeri and UniProt Accession Q46A53

for references in articles please use BRENDA:EC1.5.1.15
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Methanosarcina barkeri
UNIPROT: Q46A53 not found.
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Methanosarcina barkeri
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
mthfr, methylenetetrahydrofolate reductase, nmdmc, methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase, mthfr2, mthfr1, methylenetetrahydrofolate dehydrogenase-cyclohydrolase, msmeg_6596, msmeg_6649, nad-dependent dehydrogenase-cyclohydrolase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
bifunctional N5,N10-methylene-H4F dehydrogenase/N5,N10-methenyltetrahydrofolate cyclohydrolase
bifunctional enzyme EC 1.5.1.15/EC 3.5.4.9
FolD
bifunctional enzyme EC 1.5.1.15/EC 3.5.4.9
NAD+-dependent methylene-H4F dehydrogenase
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
5,10-methylenetetrahydrofolate:NAD+ oxidoreductase
-
CAS REGISTRY NUMBER
COMMENTARY hide
82062-90-6
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
5,10-methylenetetrahydrofolate + NAD+
5,10-methenyltetrahydrofolate + NADH + H+
show the reaction diagram
the bifunctional enzyme also shows N5,N10-methenyltetrahydrofolate cyclohydrolase activity EC 3.5.4.9. with NADP+ (1 mM), the enzyme shows less than 0.1% of the activity obtained with NAD+ (1 mM). The purified enzyme shows no activity with methylene-tetrahydromethanopterin or with 5,10-methylenetetrahydrosarcinapterin either in the presence of NAD+ or NADP+ or in the presence of F420
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NAD+
with NADP+ (1 mM), the enzyme shows less than 0.1% of the activity obtained with NAD+ (1 mM)
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.15
NAD+
pH 6.0, 37°C
additional information
5,10-methylenetetrahydrofolate
pH 6.0, 37°C, the Km-value for 5,10-methylenetetrahydrofolate in the presence of 2.7 mM NAD+ is below 0.005 mM
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1 - 2
pH 6.0, 37°C, purified enzyme, recombinant
5
pH 6.0, 37°C, extract from Escherichia coli cells carrying the expression vector
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
31000
x * 31000, SDS-PAGE
318700
x * 318700, calculated from sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
heterologously overproduced in Escherichia coli with a C-terminal His6-tag
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Buchenau, B.; Thauer, R.K.
Tetrahydrofolate-specific enzymes in Methanosarcina barkeri and growth dependence of this methanogenic archaeon on folic acid or p-aminobenzoic acid
Arch. Microbiol.
182
313-325
2004
Methanosarcina barkeri (Q46A53), Methanosarcina barkeri DSM 804 (Q46A53)
Manually annotated by BRENDA team