1.1.99.35: soluble quinoprotein glucose dehydrogenase

This is an abbreviated version!
For detailed information about soluble quinoprotein glucose dehydrogenase, go to the full flat file.

Reaction

Synonyms

2,7,9-tricarboxypyrroloquinoline quinone-dependent glucose dehydrogenase, GCD, GDH, GDHB, mGDH, PQQ dependent soluble glucose dehydrogenase, PQQ glucose dehydrogenase, PQQ-dependent glucose dehydrogenase, PQQ-GDH, PQQ-glucose dehydrogenase, PQQ-sGDH, PQQGDH, PQQGDH-B, pyrroloquinoline quinone soluble glucose dehydrogenase, pyrroloquinoline quinone-dependent glucose dehydrogenase, pyrroloquinolinequinone-dependent glucose dehydrogenase, s-GDH, sGDH, sGDH-PQQ, soluble PQQ-dependent glucose dehydrogenase, soluble PQQ-GDH, soluble PQQ-glucose dehydrogenase, soluble pyrroloquinoline quinone-dependent glucose dehydrogenase

ECTree

     1 Oxidoreductases

         1.1 Acting on the CH-OH group of donors

             1.1.99 With unknown physiological acceptors

                1.1.99.35 soluble quinoprotein glucose dehydrogenase

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Results	in table
22	AA Sequence
7	Application
7	Cloned(Commentary)
15	Cofactor
4	Crystallization (Commentary)
3	Expression
4	General Information
1	General Stability
4	Inhibitors
65	kcat/KM [mM/s]
3	Ki Value [mM]
67	KM Value [mM]
7	Localization
13	Metals/Ions
2	Molecular Weight [Da]
13	Natural Substrates/ Products (Substrates)
73	Organism
2	pH Optimum
1	Posttranslational Modification
31	Protein Variants
1	Purification (Commentary)
2	Reaction
32	Reference
2	Source Tissue
4	Specific Activity [micromol/min/mg]
94	Substrates and Products (Substrate)
5	Subunits
38	Synonyms
1	Systematic Name
7	Temperature Stability [°C]
40	Turnover Number [1/s]

Crystallization

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Crystallization on EC 1.1.99.35 - soluble quinoprotein glucose dehydrogenase

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

at 1.72 A resolution. The s-GDH monomer has a beta-propeller fold consisting of six four-stranded anti-parallel beta-sheets aligned around a pseudo 6-fold symmetry axis. The enzyme binds three calcium ions per monomer, two of which are located in the dimer interface. The third is bound in the putative active site, where it may bind and functionalize the pyrroloquinoline quinone cofactor

Acinetobacter calcoaceticus

P13650

639204

diffraction to beyond 2.1 A resolution, space group P21

Acinetobacter calcoaceticus

-

705107

structure of soluble isoform sGDH with the cofactor at 2.2 A resolution, and of its complex with reduced cofactor and D-glucose at 1.9 A resolution. Evidence for a mechanism comprisding general base-catalyzed hydride transfer

Acinetobacter calcoaceticus

-

654863

ternary complex of s-GDH with PQQ and methylhydrazine, at 1.5 A resolution. Formation of a covalent PQQ adduct in the active-site. The C5 carbonyl group of the cofactor is the most reactive moiety of PQQ. The binding of the cofactor to s-GDH is predominantly governed by polar interactions. The C2, C7, and C9 carboxyl groups of PQQ form salt bridges with Arg408, Lys377, and Arg406, respectively. The ortho-quinone O4 and O5 atoms are bound by Asn229 and Arg228, respectively. The N6, O7A, and O5 atoms of PQQ are ligands for the active-site calcium ion. The other calcium ligands are provided by the two main chain carbonyl oxygen atoms of Gly-247 and Pro-248 and two watermolecules

Acinetobacter calcoaceticus

-

639220