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Literature summary for 1.5.99.15 extracted from

  • Wang, S.; Tiongson, J.; Rasche, M.E.
    Discovery and characterization of the first archaeal dihydromethanopterin reductase, an iron-sulfur flavoprotein from Methanosarcina mazei (2014), J. Bacteriol., 196, 203-209.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Methanosarcina mazei
expression in Escherichia coli Methanocaldococcus jannaschii

General Stability

General Stability Organism
stable when frozen in liquid nitrogen Methanocaldococcus jannaschii

Metals/Ions

Metals/Ions Comment Organism Structure
Iron-sulfur cluster iron-sulfur flavoprotein Methanocaldococcus jannaschii
Iron-sulfur cluster bioinformatic analysis reveals the presence of two iron-sulfur cluster sites Methanosarcina mazei

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
29000
-
2 * 29000, SDS-PAGE Methanosarcina mazei

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
7,8-dihydromethanopterin + reduced acceptor Methanosarcina mazei the enzyme catalyzes the last step of tetrahydromethanopterin biosynthesis 5,6,7,8-tetrahydromethanopterin + oxidized acceptor
-
?
7,8-dihydromethanopterin + reduced acceptor Methanocaldococcus jannaschii the enzyme catalyzes the last step of tetrahydromethanopterin biosynthesis 5,6,7,8-tetrahydromethanopterin + oxidized acceptor
-
?
7,8-dihydromethanopterin + reduced acceptor Methanosarcina mazei DSM 3647 the enzyme catalyzes the last step of tetrahydromethanopterin biosynthesis 5,6,7,8-tetrahydromethanopterin + oxidized acceptor
-
?
7,8-dihydromethanopterin + reduced acceptor Methanocaldococcus jannaschii DSM 2661 the enzyme catalyzes the last step of tetrahydromethanopterin biosynthesis 5,6,7,8-tetrahydromethanopterin + oxidized acceptor
-
?

Organism

Organism UniProt Comment Textmining
Methanocaldococcus jannaschii Q57661
-
-
Methanocaldococcus jannaschii DSM 2661 Q57661
-
-
Methanosarcina mazei Q8PVV3
-
-
Methanosarcina mazei DSM 3647 Q8PVV3
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Methanosarcina mazei
-
Methanocaldococcus jannaschii

Storage Stability

Storage Stability Organism
labile when exposed to cold storage at 4┬░C and 20┬░C or liquid nitrogen temperatures Methanosarcina mazei

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
7,8-dihydromethanopterin + reduced acceptor the enzyme catalyzes the last step of tetrahydromethanopterin biosynthesis Methanosarcina mazei 5,6,7,8-tetrahydromethanopterin + oxidized acceptor
-
?
7,8-dihydromethanopterin + reduced acceptor the enzyme catalyzes the last step of tetrahydromethanopterin biosynthesis Methanocaldococcus jannaschii 5,6,7,8-tetrahydromethanopterin + oxidized acceptor
-
?
7,8-dihydromethanopterin + reduced acceptor the enzyme catalyzes the last step of tetrahydromethanopterin biosynthesis Methanosarcina mazei DSM 3647 5,6,7,8-tetrahydromethanopterin + oxidized acceptor
-
?
7,8-dihydromethanopterin + reduced acceptor the enzyme catalyzes the last step of tetrahydromethanopterin biosynthesis Methanocaldococcus jannaschii DSM 2661 5,6,7,8-tetrahydromethanopterin + oxidized acceptor
-
?
7,8-dihydromethanopterin + reduced dithiothreitol
-
Methanocaldococcus jannaschii 5,6,7,8-tetrahydromethanopterin + oxidized dithiothreitol
-
?
7,8-dihydromethanopterin + reduced 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 Methanosarcina mazei 5,6,7,8-tetrahydromethanopterin + oxidized dithiothreitol
-
?
7,8-dihydromethanopterin + reduced 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 Methanosarcina mazei DSM 3647 5,6,7,8-tetrahydromethanopterin + oxidized dithiothreitol
-
?
7,8-dihydromethanopterin + reduced dithiothreitol
-
Methanocaldococcus jannaschii DSM 2661 5,6,7,8-tetrahydromethanopterin + oxidized dithiothreitol
-
?

Subunits

Subunits Comment Organism
homodimer 2 * 29000, SDS-PAGE Methanosarcina mazei

Synonyms

Synonyms Comment Organism
DmrX
-
Methanosarcina mazei
DmrX
-
Methanocaldococcus jannaschii
MJ0208 locus name Methanocaldococcus jannaschii
MM1854 locus name Methanosarcina mazei

Cofactor

Cofactor Comment Organism Structure
flavin iron-sulfur flavoprotein Methanocaldococcus jannaschii
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 Methanosarcina mazei

General Information

General Information Comment Organism
physiological function the enzyme catalyzes the last step of tetrahydromethanopterin biosynthesis Methanosarcina mazei
physiological function the enzyme catalyzes the last step of tetrahydromethanopterin biosynthesis Methanocaldococcus jannaschii