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Information on EC 1.1.2.7 - methanol dehydrogenase (cytochrome c) and Organism(s) Methylophaga aminisulfidivorans MP and UniProt Accession A3FJ51

for references in articles please use BRENDA:EC1.1.2.7
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EC Tree
IUBMB Comments
A periplasmic quinoprotein alcohol dehydrogenase that only occurs in methylotrophic bacteria. It uses the novel specific cytochrome cL as acceptor. Acts on a wide range of primary alcohols, including ethanol, duodecanol, chloroethanol, cinnamyl alcohol, and also formaldehyde. Activity is stimulated by ammonia or methylamine. It is usually assayed with phenazine methosulfate. Like all other quinoprotein alcohol dehydrogenases it has an 8-bladed 'propeller' structure, a calcium ion bound to the PQQ in the active site and an unusual disulfide ring structure in close proximity to the PQQ. It differs from EC 1.1.2.8, alcohol dehydrogenase (cytochrome c), in having a high affinity for methanol and in having a second essential small subunit (no known function).
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Methylophaga aminisulfidivorans MP
UNIPROT: A3FJ51
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Word Map
The taxonomic range for the selected organisms is: Methylophaga aminisulfidivorans MP
The enzyme appears in selected viruses and cellular organisms
Synonyms
type i mdh, hd-mdh, pqq-dependent methanol dehydrogenase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SYSTEMATIC NAME
IUBMB Comments
methanol:cytochrome c oxidoreductase
A periplasmic quinoprotein alcohol dehydrogenase that only occurs in methylotrophic bacteria. It uses the novel specific cytochrome cL as acceptor. Acts on a wide range of primary alcohols, including ethanol, duodecanol, chloroethanol, cinnamyl alcohol, and also formaldehyde. Activity is stimulated by ammonia or methylamine. It is usually assayed with phenazine methosulfate. Like all other quinoprotein alcohol dehydrogenases it has an 8-bladed 'propeller' structure, a calcium ion bound to the PQQ in the active site and an unusual disulfide ring structure in close proximity to the PQQ. It differs from EC 1.1.2.8, alcohol dehydrogenase (cytochrome c), in having a high affinity for methanol and in having a second essential small subunit (no known function).
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
methanol + 2 cytochrome cL
formaldehyde + 2 reduced cytochrome cL
show the reaction diagram
A3FJ48; A3FJ51; A3FJ49
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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
methanol + 2 cytochrome cL
formaldehyde + 2 reduced cytochrome cL
show the reaction diagram
A3FJ48; A3FJ51; A3FJ49
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-
-
?
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
solute-binding protein MxaJ
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
-
1 * 18000, cytochrome cL, SDS-PAGE
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tetramer
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alpha2beta2 MDH (MDHI)
-
additional information
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ghosh, S.; Dhanasingh, I.; Ryu, J.; Kim, S.W.; Lee, S.H.
Crystal structure of cytochrome cL from the aquatic methylotrophic bacterium Methylophaga aminisulfidivorans MP
J. Microbiol. Biotechnol.
30
1261-1271
2020
Methylophaga aminisulfidivorans (A3FJ48 AND A3FJ51 AND A3FJ49), Methylophaga aminisulfidivorans MP (A3FJ48 AND A3FJ51 AND A3FJ49)
Manually annotated by BRENDA team
Myung Choi, J.; Cao, T.P.; Wouk Kim, S.; Ho Lee, K.; Haeng Lee, S.
MxaJ structure reveals a periplasmic binding protein-like architecture with unique secondary structural elements
Proteins
85
1379-1386
2017
Methylophaga aminisulfidivorans (A3FJ48 AND A3FJ51 AND A3FJ49), Methylophaga aminisulfidivorans MP (A3FJ48 AND A3FJ51 AND A3FJ49)
Manually annotated by BRENDA team