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Information on EC 1.8.98.1 - dihydromethanophenazine:CoB-CoM heterodisulfide reductase and Organism(s) Methanosarcina barkeri and UniProt Accession P96796

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IUBMB Comments
This enzyme, found in methanogenic archaea that belong to the Methanosarcinales order, regenerates CoM and CoB after the action of EC 2.8.4.1, coenzyme-B sulfoethylthiotransferase. It is a membrane-bound enzyme that contains (per heterodimeric unit) two distinct b-type hemes and two [4Fe-4S] clusters. cf. EC 1.8.7.3, ferredoxin:CoB-CoM heterodisulfide reductase, EC 1.8.98.5, H2:CoB-CoM heterodisulfide,ferredoxin reductase, EC 1.8.98.6, formate:CoB-CoM heterodisulfide,ferredoxin reductase and EC 1.8.98.4, coenzyme F420:CoB-CoM heterodisulfide,ferredoxin reductase.
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Methanosarcina barkeri
UNIPROT: P96796
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The taxonomic range for the selected organisms is: Methanosarcina barkeri
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
heterodisulfide reductase, hdrabc, hdrc2, h2:heterodisulfide oxidoreductase, hdra2b2c2, hdrc1, soluble heterodisulfide reductase, hdrb1, hdrb2, co:com-s-s-cob oxidoreductase system, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H2:heterodisulfide oxidoreductase
-
-
HdrD
-
catalytic subunit of HDR
heterodisulfide reductase
soluble heterodisulfide reductase
-
-
-
-
additional information
-
the H2:heterodisulfide oxidoreductase multienzyme complex is composed of nine polypeptides with MW 46000 Da, 39000 Da, 28000 Da, 25000 Da, 23000 Da, 21000 Da, 20000 Da, 16000 Da, 15000 Da
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
reduction
SYSTEMATIC NAME
IUBMB Comments
CoB:CoM:methanophenazine oxidoreductase
This enzyme, found in methanogenic archaea that belong to the Methanosarcinales order, regenerates CoM and CoB after the action of EC 2.8.4.1, coenzyme-B sulfoethylthiotransferase. It is a membrane-bound enzyme that contains (per heterodimeric unit) two distinct b-type hemes and two [4Fe-4S] clusters. cf. EC 1.8.7.3, ferredoxin:CoB-CoM heterodisulfide reductase, EC 1.8.98.5, H2:CoB-CoM heterodisulfide,ferredoxin reductase, EC 1.8.98.6, formate:CoB-CoM heterodisulfide,ferredoxin reductase and EC 1.8.98.4, coenzyme F420:CoB-CoM heterodisulfide,ferredoxin reductase.
CAS REGISTRY NUMBER
COMMENTARY hide
116515-35-6
-
128172-71-4
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
coenzyme B + coenzyme M + methanophenazine
N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + dihydromethanophenazine
show the reaction diagram
-
-
-
-
?
coenzyme B + coenzyme M + methylene blue
N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + reduced methylene blue
show the reaction diagram
-
-
-
-
?
CoM-S-S-CoB + ?
CoM-SH + CoB-SH + ?
show the reaction diagram
-
-
-
-
?
N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + H2
coenzyme B + coenzyme M
show the reaction diagram
N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + reduced benzyl viologen
coenzyme B + coenzyme M + benzyl viologen
show the reaction diagram
-
-
-
-
?
N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + reduced benzylviologen
coenzyme B + coenzyme M + oxidized benzyl viologen
show the reaction diagram
-
reaction intermediate is a [4Fe-4S]3+ cluster that is coordinated by one of the cysteines of nearby active-site disulfide or by the sulfur of coenzyme M
-
-
?
N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + reduced methylene blue
coenzyme B + coenzyme M + methylene blue
show the reaction diagram
-
-
-
-
r
N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + reduced methylviologen
coenzyme B + coenzyme M + methyl viologen
show the reaction diagram
-
-
-
-
?
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
N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + H2
coenzyme B + coenzyme M
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cytochrome b
the 23000 da subunit is cytochrome b
-
cytochrome b
-
additional information
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ni
-
the H2:heterodisulfide oxidoreductase multienzyme complex contains 0.6 nmol Ni per mg of protein
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,3-propanesulfone
-
0.3 mM, 50% inhibition
iodoacetamide
-
0.1 mM, 50% inhibition
NEM
-
0.4 mM, 50% inhibition
additional information
-
HDR is not inhibited by cysteine alkylating reagents at concentrations up to 2 mM
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.25
coenzyme B
-
pH 7.0, 37°C
0.8
coenzyme M
-
pH 7.0, 37°C
0.4
N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine
-
pH 7.0, 37°C, reaction with reduced benzyl viologen
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.6
-
formation of the heterodisulfide, pH 7.6, 40°C
0.62
-
reduction of the heterodisulfide, pH 7.6, 40°C
24
-
reduction of the heterodisulfide with benzylviologen
6
-
reduction of the heterodisulfide with H2
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 7.5
-
activity with reduced benzyl viologen and N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine increases continously with decreasing pH in the range between pH 7.5 and pH 5.0
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8
46000 Da subunit
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
23000
x * 23000 + x * 46000, the 230000 Da protein is cytochrome b, the 46000 Da protein is an iron-sulfur protein
46000
x * 23000 + x * 46000, the 230000 Da protein is cytochrome b, the 46000 Da protein is an iron-sulfur protein
23000
-
x * 46000 + x * 23000, the 23000 Da subunit is cytochrome b, SDS-PAGE
46000
-
x * 46000 + x * 23000, the 23000 Da subunit is cytochrome b, SDS-PAGE
additional information
-
MW of H2:heterodisulfide oxidoreductase multienzyme complex is 800000-1300000, gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 23000 + x * 46000, the 230000 Da protein is cytochrome b, the 46000 Da protein is an iron-sulfur protein
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
more stable in presence of CHAPS than in the presence of dodecyl beta-D-maltoside
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hedderich, R.; Berkessel, A.; Thauer, R.K.
Purification and properties of heterodisulfide reductase from Methanobacterium thermoautotrophicum (strain Marburg)
Eur. J. Biochem.
193
255-261
1990
Methanosarcina barkeri, Methanothermobacter thermautotrophicus, Methanothermobacter thermautotrophicus Marburg / DSM 2133
Manually annotated by BRENDA team
Heiden, S.; Hedderich, R.; Setzke, E.; Thauer, R.K.
Purification of a cytochrome b containing H2:heterodisulfide oxidoreductase complex from membranes of Methanosarcina barkeri
Eur. J. Biochem.
213
529-535
1993
Methanosarcina barkeri
Manually annotated by BRENDA team
Heiden, S.; Hedderich, R.; Setzke, E.; Thauer, R.K.
Purification of a two-subunit cytochrome-b-containing heterodisulfide reductase from methanol-grown Methanosarcina barkeri
Eur. J. Biochem.
221
855-861
1994
Methanosarcina barkeri
Manually annotated by BRENDA team
Kunkel, A.; Vaupel, M.; Heim, S.; Thauer, R.K.; Hedderich, R.
Heterodisulfide reductase from methanol-grown cells of Methanosarcina barkeri is not a flavoenzyme
Eur. J. Biochem.
244
226-234
1997
Methanosarcina barkeri (P96796), Methanosarcina barkeri
Manually annotated by BRENDA team
Madadi-Kahkesh, S.; Duin, E.C.; Heim, S.; Albracht, S.P.; Johnson, M.K.; Hedderich, R.
A paramagnetic species with unique EPR characteristics in the active site of heterodisulfide reductase from methanogenic archaea
Eur. J. Biochem.
268
2566-2577
2001
Methanosarcina barkeri, Methanothermobacter marburgensis
Manually annotated by BRENDA team
Duin, E.C.; Bauer, C.; Jaun, B.; Hedderich, R.
Coenzyme M binds to a [4Fe-4S] cluster in the active site of heterodisulfide reductase as deduced from EPR studies with the [33S]coenzyme M-treated enzyme
FEBS Lett.
538
81-84
2003
Methanosarcina barkeri, Methanothermobacter marburgensis
Manually annotated by BRENDA team
Hedderich, R.; Hamann, N.; Bennati, M.
Heterodisulfide reductase from methanogenic archaea: a new catalytic role for an iron-sulfur cluster
Biol. Chem.
386
961-970
2005
Methanosarcina barkeri, Methanosarcina thermophila, Methanothermobacter marburgensis
Manually annotated by BRENDA team