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Information on EC 1.12.98.2 - 5,10-methenyltetrahydromethanopterin hydrogenase and Organism(s) Methanopyrus kandleri and UniProt Accession Q02394

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IUBMB Comments
Does not catalyse the reduction of artificial dyes. Does not by itself catalyse a H2/H+ exchange reaction. Does not contain nickel or iron-sulfur clusters.
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Methanopyrus kandleri
UNIPROT: Q02394
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The taxonomic range for the selected organisms is: Methanopyrus kandleri
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
h2-forming methylenetetrahydromethanopterin dehydrogenase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5,10-methylene-H4MPT dehydrogenase
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Dehydrogenase, methylenetetrahydromethanopterin
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H2-forming N5,N10-Methenyltetrahydromethanopterin dehydrogenase
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Hmd
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methylenetetrahydromethanopterin dehydrogenase
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N5,N10-methenyltetrahydromethanopterin hydrogenase
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N5,N10-Methylenetetrahydromethanopterin dehydrogenase
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N5,N10-methylenetetrahydromethanopterin dehydrogenase (H2-forming)
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
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oxidation
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reduction
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SYSTEMATIC NAME
IUBMB Comments
hydrogen:5,10-methenyltetrahydromethanopterin oxidoreductase
Does not catalyse the reduction of artificial dyes. Does not by itself catalyse a H2/H+ exchange reaction. Does not contain nickel or iron-sulfur clusters.
CAS REGISTRY NUMBER
COMMENTARY hide
100357-01-5
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
N5,N10-methylenetetrahydromethanopterin + H+
N5,N10-methenyltetrahydromethanopterin + H2
show the reaction diagram
additional information
?
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the enzyme is involved in methanogenesis from CO2 and H2
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?
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
additional information
?
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the enzyme is involved in methanogenesis from CO2 and H2
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?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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tightly binds an iron-containing cofactor. The iron is coordinated by two CO molecules, one sulfur and a pyridone derivative, which is linked via a phosphodiester bond to a guanosine base
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe
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tightly binds an iron-containing cofactor. The iron is coordinated by two CO molecules, one sulfur and a pyridone derivative, which is linked via a phosphodiester bond to a guanosine base
KCl
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the enzyme requires the presence of salts, 50% of maximal activity is reached at 100 mM potassium phosphate, KCl or NaCl
NaCl
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the enzyme requires the presence of salts, 50% of maximal activity is reached at 100 mM potassium phosphate, KCl or NaCl
potassium phosphate
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the enzyme requires the presence of salts, 50% of maximal activity is reached at 100 mM potassium phosphate, KCl or NaCl
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.002
H+
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pH 5.7
0.05
N5,N10-methylenetetrahydromethanopterin
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5 - 7
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reaction rate increases hyperbolically with the proton concentration between pH 7 and pH 4.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SwissProt
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
170000
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gel filtration
44000
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4 * 44000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
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4 * 44000, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging-drop or sitting-drop, vapour diffusion method. Crystal structure of the Hmd apoenzyme from Methanocaldococcus jannaschii at 2.4 A resolution
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, under N2 gas phase, 20% loss of activity within 2 weeks
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ma, M.; Zirngibl, C.; Linder, D.; Stetter, K.O.; Thauer, R.K.
N5,N10-Methylenetetrahydromethanopterin dehydrogenase (H2-forming) from the extreme thermophile Methanopyrus kandleri
Arch. Microbiol.
156
43-48
1991
Methanopyrus kandleri
Manually annotated by BRENDA team
Pilak, O.; Mamat, B.; Vogt, S.; Hagemeier, C.H.; Thauer, R.K.; Shima, S.; Vonrhein, C.; Warkentin, E.; Ermler, U.
The Crystal structure of the apoenzyme of the iron-sulphur cluster-free hydrogenase
J. Mol. Biol.
358
798-809
2006
Methanocaldococcus jannaschii, Methanopyrus kandleri
Manually annotated by BRENDA team
Zirngibl, C.; Van Dongen, W.; Schwrer, B.; Von Bnau, R.; Richter, M.; Klein, A.; Thauer, R.K.
H2-forming methylenetetrahydromethanopterin dehydrogenase, a novel type of hydrogenase without iron-sulfur clusters in methanogenic archaea
Eur. J. Biochem.
208
511-520
1992
Methanopyrus kandleri (Q02394), Methanopyrus kandleri, Methanopyrus kandleri DSM 6324 (Q02394), Methanothermobacter marburgensis (P32440), Methanothermobacter marburgensis DSM 2133 (P32440), Methanothermobacter wolfeii (P32441), Methanothermobacter wolfeii, Methanothermobacter wolfeii DSM 2970 (P32441)
Manually annotated by BRENDA team