1.1.1.378: L-rhamnose 1-dehydrogenase [NAD(P)+]

This is an abbreviated version!
For detailed information about L-rhamnose 1-dehydrogenase [NAD(P)+], go to the full flat file.

Reaction

Synonyms

AvLRA1, AvRhaDH, EAT09360, L-rhamnose 1-dehydrogenase, LRA1, NAD(P)+-dependent L-rhamnose-1-dehydrogenase, RhaDH, SpLRA1

ECTree

1 Oxidoreductases

1.1 Acting on the CH-OH group of donors

1.1.1 With NAD⁺ or NADP⁺ as acceptor

1.1.1.378 L-rhamnose 1-dehydrogenase [NAD(P)+]

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Results	in table
30	AA Sequence
1	Cloned(Commentary)
9	Cofactor
1	Crystallization (Commentary)
5	General Information
30	kcat/KM [mM/s]
30	KM Value [mM]
1	Molecular Weight [Da]
4	Natural Substrates/ Products (Substrates)
6	Organism
7	Pathway
2	pH Optimum
9	Protein Variants
2	Purification (Commentary)
2	Reaction
5	Reference
11	Specific Activity [micromol/min/mg]
24	Substrates and Products (Substrate)
3	Subunits
11	Synonyms
1	Systematic Name
2	Temperature Optimum [°C]
30	Turnover Number [1/s]

Subunits

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Subunits on EC 1.1.1.378 - L-rhamnose 1-dehydrogenase [NAD(P)+]

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2 entries

additional information

Azotobacter vinelandii

the subunit of AvRhaDH was a single-domain protein with an alpha/beta doubly wound structure. A seven-stranded parallel beta-sheet (beta3-beta2-beta1-beta4-beta5-beta6-beta7) in the center of the molecule is sandwiched by two arrays of parallel alpha-helices (alpha1 to alpha6), which is a typical dinucleotide binding the Rossmann fold motif including the characteristic sequence Gly-X3-Gly-X-Gly; Gly12-Ala13-Ser14-Arg15-Gly16-Ile17-Gly18. Furthermore, a motif corresponding to Asn92-Asn93-Ala94-Gly95 is previously shown to be important for stabilizing this central beta-sheet in other SDR superfamily enzymes. A small domain containing the alpha7 and two 310 helixes is slightly separated from the main body of the subunit, and contained the flexible region

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