1.1.1.3: homoserine dehydrogenase
This is an abbreviated version!
For detailed information about homoserine dehydrogenase, go to the full flat file.
Word Map on EC 1.1.1.3
-
1.1.1.3
-
l-threonine
-
threonine-sensitive
-
corynebacterium
-
glutamicum
-
l-lysine
-
semialdehyde
-
dihydrodipicolinate
-
l-isoleucine
-
brevibacterium
-
aspartate-derived
-
2.7.2.4
-
i-homoserine
-
rhodospirillum
-
lysine-sensitive
-
lactofermentum
-
feedback-insensitive
-
feedback-resistant
-
synthesis
-
drug development
-
agriculture
-
pharmacology
- 1.1.1.3
- l-threonine
-
threonine-sensitive
- corynebacterium
- glutamicum
- l-lysine
- semialdehyde
- dihydrodipicolinate
- l-isoleucine
- brevibacterium
-
aspartate-derived
-
2.7.2.4
-
i-homoserine
-
rhodospirillum
-
lysine-sensitive
- lactofermentum
-
feedback-insensitive
-
feedback-resistant
- synthesis
- drug development
- agriculture
- pharmacology
Reaction
Synonyms
AK-HDH, AK-HSD-1, AK-HSDH, AK-HseDH, aspartate kinase-homoserine dehydrogenase, aspartokinase-homoserine dehydrogenase I, bifunctional aspartate kinase-homoserine dehydrogenase, BsHSD, HDH, hom, hom-1, Hom6, homoserine dehydrogenase 1, homoserine dehydrogenase 2, HSD, HSDH, HseDH, More, orf19.2951, PbHSD, SACOL1362, StHSD, thrA, TM_0547, TTHA0489, TtHSD
ECTree
Advanced search results
Activating Compound
Activating Compound on EC 1.1.1.3 - homoserine dehydrogenase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
dithiothreitol
the enzyme is 2.5fold activated by the addition of 0.8 mM dithiothreitol. The activation is caused by cleavage of the disulfide bond formed between two cysteine residues in the C-terminal regions of the two subunits
the HSD from the hyperthermophilic archaeon Sulfolobus tokodaii (StHSD) is activated by reductive cleavage of the disulfide bond formed between cysteine residues (Cys304) in the C-terminal regions of the homodimer subunits
-
additional information
-
the HSD from the hyperthermophilic archaeon Sulfolobus tokodaii (StHSD) is activated by reductive cleavage of the disulfide bond formed between cysteine residues (Cys304) in the C-terminal regions of the homodimer subunits
-