Cloned (Comment) | Organism |
---|---|
- |
Oryza sativa Japonica Group |
Crystallization (Comment) | Organism |
---|---|
structures in the presence of cofactors, NAD+ and NADP+, and complexed with ascorbic acid and isoascorbic acid. The overall structure of MDHAR is similar to other iron-sulfur protein reductases, except for a unique long loop of 63-80 residues, which seems to be essential in forming the active site pocket. Residue Arg320 plays a major substrate binding role, and Tyr349 mediates electron transfer from NAD(P)H to bound substrate via FAD. The enzymatic activity favours NADH as an electron donor over NADPH | Oryza sativa Japonica Group |
Protein Variants | Comment | Organism |
---|---|---|
C70A | about 105% of wild-type activity | Oryza sativa Japonica Group |
E196A | residue E196 forms a hydrogen bond to the O2B molecule in the adenosine ring of NAD. Mutation reduces catalytic activity. Mutant E196A has only about 3 times higher affinity for NAD than that for NADP, i.e. 16fold increase in affinity for NADP compared to the wild-type | Oryza sativa Japonica Group |
G72N | about 70% of wild-type activity | Oryza sativa Japonica Group |
R320A | about 20% of wild-type activity | Oryza sativa Japonica Group |
Y349A | about 10% of wild-type activity | Oryza sativa Japonica Group |
Y349F | about 10% of wild-type activity | Oryza sativa Japonica Group |
Y349W | about 10% of wild-type activity | Oryza sativa Japonica Group |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Oryza sativa Japonica Group | Q652L6 | - |
- |
Synonyms | Comment | Organism |
---|---|---|
Os09g0567300 | - |
Oryza sativa Japonica Group |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NADH | - |
Oryza sativa Japonica Group | |
NADPH | about 50% of the activity with NADH | Oryza sativa Japonica Group |