CATH Classification
Level | CATH Code | Description |
---|---|---|
3 | Alpha Beta | |
3.30 | 2-Layer Sandwich | |
3.30.360 | Dihydrodipicolinate Reductase; domain 2 | |
3.30.360.10 | Dihydrodipicolinate Reductase; domain 2 |
Domain Context
CATH Clusters
Superfamily | Dihydrodipicolinate Reductase; domain 2 |
Functional Family | Galactose 1-dehydrogenase |
Enzyme Information
1.1.1.376 |
L-arabinose 1-dehydrogenase (NAD(P)(+)).
based on mapping to UniProt Q53TZ2
L-arabinose + NAD(P)(+) = L-arabinono-1,4-lactone + NAD(P)H.
-!- The enzymes from the bacterium Azospirillum brasilense and the archaeon Haloferax volcanii are part of the L-arabinose degradation pathway and prefer NADP(+) over NAD(+). -!- In vitro the enzyme from Azospirillum brasilense shows also high catalytic efficiency with D-galactose.
|
1.1.1.48 |
D-galactose 1-dehydrogenase.
based on mapping to UniProt Q53TZ2
D-galactose + NAD(+) = D-galactono-1,4-lactone + NADH.
-!- This enzyme is part of the De Ley-Doudoroff pathway, which is used by some bacteria during growth on D-galactose.
|
1.1.1.120 |
Galactose 1-dehydrogenase (NADP(+)).
based on mapping to UniProt Q53TZ2
D-galactose + NADP(+) = D-galactono-1,5-lactone + NADPH.
-!- Also acts on L-arabinose, 6-deoxy- and 2-deoxy-D-galactose.
|
UniProtKB Entries (1)
Q53TZ2 |
ARAA_AZOBR
Azospirillum brasilense
L-arabinose 1-dehydrogenase (NAD(P)(+))
|
PDB Structure
PDB | 6JNK |
External Links | |
Method | X-RAY DIFFRACTION |
Organism | |
Primary Citation |
Structural insights into the catalytic and substrate recognition mechanisms of bacterial l-arabinose 1-dehydrogenase.
Febs Lett.
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