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Information on EC 1.12.98.2 - 5,10-methenyltetrahydromethanopterin hydrogenase and Organism(s) Methanothermobacter marburgensis and UniProt Accession P32440

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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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Methanothermobacter marburgensis
UNIPROT: P32440
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The taxonomic range for the selected organisms is: Methanothermobacter marburgensis
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
h2-forming methylenetetrahydromethanopterin dehydrogenase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H2-forming methylenetetrahydromethanopterin dehydrogenase
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5,10-methylene-H4MPT dehydrogenase
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-
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Dehydrogenase, methylenetetrahydromethanopterin
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H2-forming N5,N10-Methenyltetrahydromethanopterin dehydrogenase
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-
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Hmd
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-
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methylenetetrahydromethanopterin dehydrogenase
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-
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N5,N10-methenyltetrahydromethanopterin hydrogenase
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-
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N5,N10-Methylenetetrahydromethanopterin dehydrogenase
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-
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N5,N10-methylenetetrahydromethanopterin dehydrogenase (H2-forming)
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-
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-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
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-
-
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oxidation
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-
-
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reduction
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-
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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
H+ + 5,10-methylenetetrahydromethanopterin
H2 + 5,10-methenyltetrahydromethanopterin
show the reaction diagram
the purified enzyme does not catalyze the reduction of viologen dyes, of methylene blue, of flavins, of pyridine nucleotides
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-
r
5,10-methenyltetrahydromethanopterin + H2
5,10-methylenetetrahydromethanopterin + H+
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
5,10-methenyltetrahydromethanopterin + H2
5,10-methylenetetrahydromethanopterin + H+
show the reaction diagram
-
involved in methanogenesis
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-
r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Zn2+
the zinc content varies from preparation to preparation between 0.5-4 mol zinc/mol enzyme
additional information
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cyanide
1 mM, 50% inhibition
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.05
5,10-methenyltetrahydromethanopterin
pH 7.5, 60°C
0.04
5,10-methylenetetrahydromethanopterin
pH 6.5, 60°C
additional information
H2
the apparent Km for H2 is estimated to be approximately 60% H2 in the gas phase
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
975
5,10-methenyltetrahydromethanopterin
pH 7.5, 60°C
1462
5,10-methylenetetrahydromethanopterin
pH 6.5, 60°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.1 - 0.2
CN-
0.01
CO
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pH 6.0, 40°C, under N2
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
610
-
purified enzyme, pH 6.0, 40°C, under N2
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60
in 120 mM potassium phosphate pH 6
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40 - 65
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2.5-fold higher activity at 65°C than at 40°C
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.4
isoelectric focussing
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40000
-
2 * 40000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
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2 * 40000, SDS-PAGE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60
30 min, 50% inactivation
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
enzyme and cofactor are light sensitive
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sensitive to UV-A/blue light, CO protects from inactivation
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
rapidly inactivated in the presence of molecular oxygen. The rate of inactivation increases in the presence of dithiothreitol (2 mM) or of mercaptoethanol (5 mM)
727402
enzyme is rapidly inactivated upon exposure to oxygen
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658635
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
all purification steps are performed in the dark
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Lyon, E.J.; Shima, S.; Buurman, G.; Chowdhuri, S.; Batschauer, A.; Steinbach, K.; Thauer, R.K.
UV-A/blue-light inactivation of the metal-free hydrogenase (Hmd) from methanogenic archaea. The enzyme contains functional iron after all
Eur. J. Biochem.
271
195-204
2004
Methanocaldococcus jannaschii, Methanothermobacter marburgensis
Manually annotated by BRENDA team
Bartoschek, S.; Buurman, G.; Geierstanger, B.H.; Lapham, J.; Griesinger, C.
Measurement and ab initio calculation of CSA/dipole-dipole cross-correlated relaxation provide insight into the mechanism of a H2-forming dehydrogenase
J. Am. Chem. Soc.
125
13308-13309
2003
Methanothermobacter marburgensis
Manually annotated by BRENDA team
Lyon, E.J.; Shima, S.; Boecher, R.; Thauer, R.K.; Grevels, F.W.; Bill, E.; Roseboom, W.; Albracht, S.P.J.
Carbon monoxide as an intrinsic ligand to iron in the active site of the iron-sulfur-cluster-free hydrogenase H2-forming methylenetetrahydromethanopterin dehydrogenase as revealed by infrared spectroscopy
J. Am. Chem. Soc.
126
14239-14248
2004
Methanothermobacter marburgensis
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