1.5.99.14: 6-hydroxypseudooxynicotine dehydrogenase

This is an abbreviated version!
For detailed information about 6-hydroxypseudooxynicotine dehydrogenase, go to the full flat file.

Reaction

Synonyms

KdhA, KdhB, KdhC, KdhL, KdhM, KdhS, PNO

ECTree

     1 Oxidoreductases

         1.5 Acting on the CH-NH group of donors

             1.5.99 With unknown physiological acceptors

                1.5.99.14 6-hydroxypseudooxynicotine dehydrogenase

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All data fields related to EC 1.5.99.14

Results	in table
254	AA Sequence
2	Cloned(Commentary)
7	Cofactor
1	Crystallization (Commentary)
4	General Information
10	kcat/KM [mM/s]
10	KM Value [mM]
2	Metals/Ions
4	Molecular Weight [Da]
2	Natural Substrates/ Products (Substrates)
21	Organism
4	Pathway
6	PDB ID
5	Protein Variants
1	Purification (Commentary)
1	Reaction
9	Reference
1	Specific Activity [micromol/min/mg]
10	Substrates and Products (Substrate)
3	Subunits
9	Synonyms
1	Systematic Name
10	Turnover Number [1/s]

Crystallization

Crystallization on EC 1.5.99.14 - 6-hydroxypseudooxynicotine dehydrogenase

for references in articles please use BRENDA:EC1.5.99.14

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

structure of the Kdh holoenzyme, with its three subunits KdhL, KdhM, and KdhS, and their associated cofactors molybdopterin cytosine dinucleotide, two iron-sulfur clusters (Fe2S2), and flavin adenine dinucleotide, respectively. The residues Glu345, Try551, and Glu748 of KdhL participate in substrate binding, and Phe269 and Arg383 of KdhL contribute to stabilize the molybdopterin cytosine dinucleotide conformation

Paenarthrobacter nicotinovorans

O87681; O87682; Q933N0

765432