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Information on EC 1.5.99.15 - dihydromethanopterin reductase (acceptor) Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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The expected taxonomic range for this enzyme is: Euryarchaeota
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dihydromethanopterin reductase (acceptor)
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5,6,7,8-tetrahydromethanopterin + oxidized acceptor = 7,8-dihydromethanopterin + reduced acceptor
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tetrahydromethanopterin biosynthesis
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methanogenesis from CO2
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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)+].
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DmrX
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MJ0208
locus name
MM1854
locus name
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UniProt
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UniProt
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UniProt
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UniProt
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physiological function
the enzyme catalyzes the last step of tetrahydromethanopterin biosynthesis
physiological function
the enzyme catalyzes the last step of tetrahydromethanopterin biosynthesis
physiological function
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the enzyme catalyzes the last step of tetrahydromethanopterin biosynthesis
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physiological function
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the enzyme catalyzes the last step of tetrahydromethanopterin biosynthesis
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7,8-dihydromethanopterin + reduced acceptor
5,6,7,8-tetrahydromethanopterin + oxidized acceptor
7,8-dihydromethanopterin + reduced dithiothreitol
5,6,7,8-tetrahydromethanopterin + oxidized dithiothreitol
7,8-dihydromethanopterin + reduced acceptor
5,6,7,8-tetrahydromethanopterin + oxidized acceptor
the enzyme catalyzes the last step of tetrahydromethanopterin biosynthesis
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7,8-dihydromethanopterin + reduced acceptor
5,6,7,8-tetrahydromethanopterin + oxidized acceptor
the enzyme catalyzes the last step of tetrahydromethanopterin biosynthesis
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7,8-dihydromethanopterin + reduced acceptor
5,6,7,8-tetrahydromethanopterin + oxidized acceptor
the enzyme catalyzes the last step of tetrahydromethanopterin biosynthesis
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7,8-dihydromethanopterin + reduced acceptor
5,6,7,8-tetrahydromethanopterin + oxidized acceptor
the enzyme catalyzes the last step of tetrahydromethanopterin biosynthesis
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7,8-dihydromethanopterin + reduced dithiothreitol
5,6,7,8-tetrahydromethanopterin + oxidized dithiothreitol
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7,8-dihydromethanopterin + reduced dithiothreitol
5,6,7,8-tetrahydromethanopterin + oxidized dithiothreitol
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7,8-dihydromethanopterin + reduced dithiothreitol
5,6,7,8-tetrahydromethanopterin + oxidized dithiothreitol
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
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7,8-dihydromethanopterin + reduced dithiothreitol
5,6,7,8-tetrahydromethanopterin + oxidized dithiothreitol
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
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7,8-dihydromethanopterin + reduced acceptor
5,6,7,8-tetrahydromethanopterin + oxidized acceptor
7,8-dihydromethanopterin + reduced acceptor
5,6,7,8-tetrahydromethanopterin + oxidized acceptor
Q57661
the enzyme catalyzes the last step of tetrahydromethanopterin biosynthesis
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7,8-dihydromethanopterin + reduced acceptor
5,6,7,8-tetrahydromethanopterin + oxidized acceptor
Q57661
the enzyme catalyzes the last step of tetrahydromethanopterin biosynthesis
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7,8-dihydromethanopterin + reduced acceptor
5,6,7,8-tetrahydromethanopterin + oxidized acceptor
Q8PVV3
the enzyme catalyzes the last step of tetrahydromethanopterin biosynthesis
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7,8-dihydromethanopterin + reduced acceptor
5,6,7,8-tetrahydromethanopterin + oxidized acceptor
Q8PVV3
the enzyme catalyzes the last step of tetrahydromethanopterin biosynthesis
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flavin
iron-sulfur flavoprotein
FMN
bioinformatic analysis reveals the presence of one FMN-binding site. The purified protein shows an absorbance peaks at 380 and 460 nm, characteristic of oxidized FMN
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Iron-sulfur cluster
iron-sulfur flavoprotein
Iron-sulfur cluster
bioinformatic analysis reveals the presence of two iron-sulfur cluster sites
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29000
2 * 29000, SDS-PAGE
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homodimer
2 * 29000, SDS-PAGE
homodimer
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2 * 29000, SDS-PAGE
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stable when frozen in liquid nitrogen
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labile when exposed to cold storage at 4°C and 20°C or liquid nitrogen temperatures
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expression in Escherichia coli
expression in Escherichia coli
expression in Escherichia coli
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DMRX_METJA
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
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27697
Swiss-Prot
DMRX_METMA
Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)
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26491
Swiss-Prot
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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, Methanocaldococcus jannaschii (Q57661), Methanocaldococcus jannaschii DSM 2661 (Q57661), Methanosarcina mazei, Methanosarcina mazei (Q8PVV3), Methanosarcina mazei DSM 3647 (Q8PVV3)
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