1.1.2.7: methanol dehydrogenase (cytochrome c)
This is an abbreviated version!
For detailed information about methanol dehydrogenase (cytochrome c), go to the full flat file.
Word Map on EC 1.1.2.7
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1.1.2.7
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1.1.99.8
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phenazine
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methylamine
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formaldehyde
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hyphomicrobium
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quinoproteins
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pyrroloquinoline
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methylophilus
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denitrificans
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paracoccus
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methylotrophus
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half-reaction
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linewidth
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quinone-dependent
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methylobacterium
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protiated
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wurster
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methylomonas
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one-electron
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extorquens
- 1.1.2.7
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1.1.99.8
- phenazine
- methylamine
- formaldehyde
- hyphomicrobium
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quinoproteins
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pyrroloquinoline
- methylophilus
- denitrificans
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paracoccus
- methylotrophus
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half-reaction
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linewidth
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quinone-dependent
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methylobacterium
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protiated
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wurster
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methylomonas
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one-electron
- extorquens
Reaction
+ 2 ferricytochrome cL = + 2 ferrocytochrome cL + 2 H+
Synonyms
EC 1.1.99.8, Hd-MDH, MDH, MDH2, MEDH, methanol dehydrogenase, More, mxaF, MxaJ, PQQ-dependent methanol dehydrogenase, pyrroloquinoline quinone-dependent quinoprotein methanol dehydrogenase, QH-ADH, QMDH, quinohemoprotein (type II) alcohol dehydrogenase, quinohemoprotein alcohol dehydrogenase, quinone-dependent alcohol dehydrogenase, quinoprotein alcohol dehydrogenase, quinoprotein dehydrogenase, quinoprotein methanol dehydrogenase, type I MDH, type II MDH
ECTree
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Cofactor
Cofactor on EC 1.1.2.7 - methanol dehydrogenase (cytochrome c)
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2,7,9-tricarboxypyrroloquinoline quinone
PQQ, tetrahedral configuration of the C-5 atom of PQQ, configuration and binding structure, overview
cytochrome cL
flow of electrons from reduced pyrroloquinoline quinone to the heme of cytochrome cL, binding and crystal structure determination and analysis at 1.6 A resolution, contains a disulfide bridge that tethers the long C-terminal extension to the body of the structure, overview
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cytochrome cL
Ma-CytcL, contains heme c and has unique features compared to those of the terrestrial homologues. Apart from Fe2+ in heme, three additional metal ion binding sites for Na+, Ca2+, and Fe2+ are found, wherein the ions mostly form coordination bonds with the amino acid residues on the loop (G93-Y111) that interacts with heme. These ions seem to enhance the stability of heme insertion by increasing the loop's steadiness. The basic N-terminal end, together with helix alpha4 and loop G126-Y136, contributes positive charge to the region. In contrast, the acidic C-terminal end provides a negatively charged surface, yielding several electrostatic contact points with partner proteins for electron transfer. The need for an adapter protein bridging MDH to CytcL within appropriate proximity for electron transfer is satisfied by protein MxaJ. Native Ma-CytcL is purified from Methylophaga aminisulfidivorans cell culture by anion exchange chromatography and gel filtration. It contains a signal peptide, sequence comparisons and metal binding sites analysis, overview
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heme c
coordination in CtcL at the active site, structure, overview. Contains Fe2+
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mediates reduction of 2,6-dichlorophenol-indophenol
phenazine methosulfate
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mediates reduction of 2,6-dichlorophenolindophenol
pyrroloquinoline quinone
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bound to the enzyme, preparation of Ca2+-free MDH, which contains a fully-oxidized pyrroloquinoline quinone cofactor, incubation of Ca2+-free MDH with Ca2+ ion leads to reconstituted, fully active enzyme containing fully-reduced, tightly bound PQQ, overview
pyrroloquinoline quinone
i.e. PQQ or 4,5-dihydro-4,5-dioxo-1H-pyrrolo[2,3-f]quinoline-2,7,9-tricarboxylaic acid, enzyme-bound to the active site, 1 molecule per alpha-subunit, required for catalytic activity
pyrroloquinoline quinone
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i.e. PQQ or 4,5-dihydro-4,5-dioxo-1H-pyrrolo[2,3-f]quinoline-2,7,9-tricarboxylaic acid, enzyme-bound, required for catalytic activity, the cofactor is located in a cavity near to the end of an A strand, and it is sandwiched between the indole ring of the residue Trp237 and the S-S bridge of the couple Cys103-Cys104
pyrroloquinoline quinone
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the enzyme is a type II PQQ-containing alcohol dehydrogenase, the cofactor is bound to the active site in an entirely planar conformation of the tricyclic PQQ cofactor ring, binding structure overview
pyrroloquinoline quinone
binding structure in the active site, overview
pyrroloquinoline quinone
dependent on, prosthetic group, the PQQ in the active site is held in place by a coplanar tryptophan and by a novel disulfide ring formed between adjacent cysteines which are bonded by an unusual non-planar trans peptide bond. One of the carbonyl oxygens of PQQ is bonded to the Ca2+ , probably facilitating attack on the substrate, and the other carbonyl oxygen is out of the plane of the ring, confirming the presence of the predicted free-radical semiquinone form of the prosthetic group
pyrroloquinoline quinone
flow of electrons from reduced pyrroloquinoline quinone to the heme of cytochrome cL, binding structure
pyrroloquinoline quinone
i.e. 2,7,9-tricarboxy-1H-pyrrolo[2,3-f]quinoline-4,5-dione, PQQ, structures of anionic PQQ, neutral PQQ, and reduced PQQ, overview
pyrroloquinoline quinone
i.e. 2,7,9-tricarboxy-1H-pyrrolo[2,3-f]quinoline-4,5-dione, PQQ, structures of anionic PQQ, neutral PQQ, and reduced PQQ, overview
pyrroloquinoline quinone
PQQ, binding structure at the active site, overview, the active site contains a single Ca2 + ion whose coordination sphere contains PQQ and protein atoms, including both oxygens of the carboxylate of Glu177 and the amide oxygen of Asn261
pyrroloquinoline quinone
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PQQ, serves as the redox cofactor in bacterial MEDH, PQQ is located in a central channel of the disk-shaped protein, and is sandwiched between a Trp side chain and a very unusual vicinal disulfide, binding structure, overview
pyrroloquinoline quinone
PQQ, tetrahedral configuration of the C-5 atom of PQQ, configuration and binding structure at the active site, ab initio structures of 2,7,9-tricarboxypyrroloquinoline quinone, semiquinone, and dihydroquinone, free and in complex with Ca2+, overview
pyrroloquinoline quinone
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prosthetic group, 1.3 molecules per enzyme molecule
pyrroloquinoline quinone
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enzyme contains two semiquinone pyrroloquinoline quinone groups per heterotetramer
pyrroloquinoline quinone
PQQ, 2 mol of PQQ per mol of enzyme, the cofactor is predominantly in the semiquinone form, binding structure, overview
pyrroloquinoline quinone
PQQ, is the only prosthetic group, the PQQ is sandwiched between the indole ring of Trp243 and the disulfide ring structure, overview
pyrroloquinoline quinone
PQQ, one molecule per enzyme alpha-subunit. The PQQ ring is sandwiched between the indole ring of Trp243 and the two sulphur atoms of the disulfide ring structure
pyrroloquinoline quinone
the pyrroloquinoline quinone prosthetic group is located in the central channel of the large subunit near the surface of the molecule
pyrroloquinoline quinone
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i.e. PQQ or 4,5-dihydro-4,5-dioxo-1H-pyrrolo[2,3f]quinoline-2,7,9-tricarboxylic acid, essentially required, binding structure
pyrroloquinoline quinone
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i.e. PQQ or 4,5-dihydro-4,5-dioxo-1H-pyrrolo[2,3f]quinoline-2,7,9-tricarboxylic acid, essentially required, binding structure
pyrroloquinoline quinone
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i.e. PQQ or 4,5-dihydro-4,5-dioxo-1H-pyrrolo[2,3f]quinoline-2,7,9-tricarboxylic acid, essentially required, binding structure
pyrroloquinoline quinone
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i.e. PQQ or 4,5-dihydro-4,5-dioxo-1H-pyrrolo[2,3f]quinoline-2,7,9-tricarboxylic acid, essentially required, binding structure
pyrroloquinoline quinone
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i.e. PQQ or 4,5-dihydro-4,5-dioxo-1H-pyrrolo[2,3f]quinoline-2,7,9-tricarboxylic acid, essentially required, binding structure
pyrroloquinoline quinone
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i.e. PQQ or 4,5-dihydro-4,5-dioxo-1H-pyrrolo[2,3f]quinoline-2,7,9-tricarboxylic acid, essentially required, binding structure
pyrroloquinoline quinone
Diplococcus sp.
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i.e. PQQ or 4,5-dihydro-4,5-dioxo-1H-pyrrolo[2,3f]quinoline-2,7,9-tricarboxylic acid, essentially required, binding structure
pyrroloquinoline quinone
the enzyme contains the prosthetic group pyrroloquinoline quinone, PQQ, non-covalently bound, which catalyzes the oxidation of methanol to formaldehyde, two molecules per enzyme tetramer, chemical structure and configuration change of PQQ., overview
pyrroloquinoline quinone
PQQ, active site bound
an NAD(P)-independent enzyme
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additional information
an NAD(P)-independent enzyme
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additional information
Ma-MxaJ contains the bi-lobate folding architecture found in periplasmic binding proteins (PDB ID 5SV6), presence of an acidic cavity at the interface of the two domains
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additional information
MxaJ, a chaperone-like protein facilitating the assembly of MDH, additional component MxaJ together with a MDHI can facilitate the methanol oxidation process
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