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Information on EC 1.5.99.15 - dihydromethanopterin reductase (acceptor) and Organism(s) Methanosarcina mazei and UniProt Accession Q8PVV3

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IUBMB Comments
This archaeal enzyme catalyses the last step in the biosynthesis of tetrahydromethanopterin, a coenzyme used in methanogenesis. The enzyme, characterized from the archaea Methanosarcina mazei and Methanocaldococcus jannaschii, is an iron-sulfur flavoprotein. cf. EC 1.5.1.47, dihydromethanopterin reductase [NAD(P)+].
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Methanosarcina mazei
UNIPROT: Q8PVV3
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The taxonomic range for the selected organisms is: Methanosarcina mazei
The expected taxonomic range for this enzyme is: Archaea, Bacteria
Synonyms
mm1854, mj0208, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
methylene H4MPT dehydrogenase B
-
MM1854
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
5,6,7,8-tetrahydromethanopterin:acceptor 5,6-oxidoreductase
This archaeal enzyme catalyses the last step in the biosynthesis of tetrahydromethanopterin, a coenzyme used in methanogenesis. The enzyme, characterized from the archaea Methanosarcina mazei and Methanocaldococcus jannaschii, is an iron-sulfur flavoprotein. cf. EC 1.5.1.47, dihydromethanopterin reductase [NAD(P)+].
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
7,8-dihydromethanopterin + reduced acceptor
5,6,7,8-tetrahydromethanopterin + oxidized acceptor
show the reaction diagram
the enzyme catalyzes the last step of tetrahydromethanopterin biosynthesis
-
-
?
7,8-dihydromethanopterin + reduced dithiothreitol
5,6,7,8-tetrahydromethanopterin + oxidized dithiothreitol
show the reaction diagram
NAD(P)H is incapable of directly reducing the flavin cofactor, but dithionite eliminates the FMN peaks, indicating successful electron transfer to the enzyme. An electron transfer system of NADPH, spinach NADPH-ferredoxin oxidoreductase, and ferredoxin can also reduce the FMN peaks. A newly developed assay indicates that dithiothreitol-reduced enzyme can transfer electrons to dihydromethanopterin. Ferredoxin may serve as an electron donor
-
-
?
7,8-dihydromethanopterin + reduced ferredoxin
5,6,7,8-tetrahydromethanopterin + ferredoxin
show the reaction diagram
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
7,8-dihydromethanopterin + reduced acceptor
5,6,7,8-tetrahydromethanopterin + oxidized acceptor
show the reaction diagram
the enzyme catalyzes the last step of tetrahydromethanopterin biosynthesis
-
-
?
7,8-dihydromethanopterin + reduced ferredoxin
5,6,7,8-tetrahydromethanopterin + ferredoxin
show the reaction diagram
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ferredoxin
ferredoxin may serve as an electron donor
-
[4Fe-4S]-center
the enzyme contains two iron-sulfur cluster sites
additional information
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe2+
the enzyme contains two [4Fe-4S] cluster sites
Iron-sulfur cluster
bioinformatic analysis reveals the presence of two iron-sulfur cluster sites
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
assay at room temperature
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
the microbial production of methane by methanogenic archaea is dependent on the synthesis of the pterin-containing cofactor tetrahydromethanopterin (H4MPT). The enzyme catalyzing the last step of H4MPT biosynthesis is dihydromethanopterin reductase
physiological function
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
29000
2 * 29000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100
purified recombinant His-tagged enzyme, pH 7.0, 15 min, inactivation
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
labile when exposed to cold storage at 4°C and 20°C or liquid nitrogen temperatures
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His6-tagged enzyme from Escherichia coli strain BE100 [BL21(DE3) RIL] in an anaerobic chamber by nickel affinity chromatography, ultrafiltration, and gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
gene dmrX, recombinant expression of His6-tagged enzyme in Escherichia coli strain BE100 [BL21(DE3) RIL]
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wang, S.; Tiongson, J.; Rasche, M.E.
Discovery and characterization of the first archaeal dihydromethanopterin reductase, an iron-sulfur flavoprotein from Methanosarcina mazei
J. Bacteriol.
196
203-209
2014
Methanocaldococcus jannaschii (Q57661), Methanocaldococcus jannaschii, Methanocaldococcus jannaschii DSM 2661 (Q57661), Methanosarcina mazei (Q8PVV3), Methanosarcina mazei, Methanosarcina mazei DSM 3647 (Q8PVV3)
Manually annotated by BRENDA team
Wang, S.; Tiongson, J.; Rasche, M.E.
Discovery and characterization of the first archaeal dihydromethanopterin reductase, an iron-sulfur flavoprotein from Methanosarcina mazei
J. Bacteriol.
196
203-209
2014
Methanocaldococcus jannaschii (Q57661), Methanocaldococcus jannaschii, Methanocaldococcus jannaschii DSM 2661 (Q57661), Methanosarcina mazei (Q8PVV3), Methanosarcina mazei, Methanosarcina mazei DSM 3647 (Q8PVV3)
Manually annotated by BRENDA team