1.17.1.8: 4-hydroxy-tetrahydrodipicolinate reductase
This is an abbreviated version!
For detailed information about 4-hydroxy-tetrahydrodipicolinate reductase, go to the full flat file.
Word Map on EC 1.17.1.8
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1.17.1.8
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diaminopimelate
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glutamicum
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meso-diaminopimelate
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aspartokinase
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imine
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dhdps
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2,6-pyridinedicarboxylate
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medicine
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alpha,beta-unsaturated
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2'-phosphate
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s-2-aminoethyl-l-cysteine
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aspartate-semialdehyde
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drug development
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agriculture
- 1.17.1.8
- diaminopimelate
- glutamicum
- meso-diaminopimelate
- aspartokinase
- imine
- dhdps
- 2,6-pyridinedicarboxylate
- medicine
-
alpha,beta-unsaturated
-
2'-phosphate
- s-2-aminoethyl-l-cysteine
-
aspartate-semialdehyde
- drug development
- agriculture
Reaction
Synonyms
AbDHDPR, CRR1, DapB, DHDP reductase, DHDPR, DHPR, dihydrodipicolinate reductase, dihydrodipicolinate reductase-like protein, dihydrodipicolinic acid reductase, EC 1.3.1.26, MRSA-DHDPR, reductase, dihydrodipicolinate
ECTree
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Engineering
Engineering on EC 1.17.1.8 - 4-hydroxy-tetrahydrodipicolinate reductase
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K11A
site-directed mutagenesis, increased activity with and specificty for NADH as cofactor, reduced activity with NADPH compared to the wild-type enzyme
K9A
site-directed mutagenesis, increased specificty for NADH as cofactor, reduced activity with NADPH compared to the wild-type enzyme
K11A
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site-directed mutagenesis, increased activity with and specificty for NADH as cofactor, reduced activity with NADPH compared to the wild-type enzyme
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K9A
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site-directed mutagenesis, increased specificty for NADH as cofactor, reduced activity with NADPH compared to the wild-type enzyme
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K35A
additional information
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natural mutant strain GR45B with an additional plasmid encoded dapB gene evokes a different phenotype in alfalfa plants after nodulation, yellow plants in nitrogen-free medium
the mutation does not alter the oligomeric status or spectroscopic properties of the enzyme, however, NADPH binding is altered by ca 20fold with much less change (ca 4fold) in NADH binding compared to the wild type enzyme
K35A
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the mutation does not alter the oligomeric status or spectroscopic properties of the enzyme, however, NADPH binding is altered by ca 20fold with much less change (ca 4fold) in NADH binding compared to the wild type enzyme
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