1.5.1.17: alanopine dehydrogenase
This is an abbreviated version!
For detailed information about alanopine dehydrogenase, go to the full flat file.
Word Map on EC 1.5.1.17
-
1.5.1.17
-
analysis
-
fulgidus
-
1.4.1.1
-
archaeoglobus
-
proteolyticus
-
cyclodeaminase
-
phormidium
-
octopine
-
diagnostics
- 1.5.1.17
- analysis
- fulgidus
-
1.4.1.1
- archaeoglobus
- proteolyticus
-
cyclodeaminase
-
phormidium
- octopine
- diagnostics
Reaction
Synonyms
ADH, ALADH, AlaDHAm, ALPDH, Dehydrogenase, alanopine, meso-N-(1-Carboxyethyl)-alanine dehydrogenase
ECTree
1.5.1.17 alanopine dehydrogenaseAdvanced search results
results (
results (General Information
General Information on EC 1.5.1.17 - alanopine dehydrogenase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
top
GENERAL INFORMATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
evolution
AlaDHAm is a member of the family of opine dehydrogenases (OpDHs), which catalyze the reductive condensation of pyruvate with an L-amino acid in the presence of NADH to so-called opines during anaerobic glycolysis. Residue E141 of domain I and W279 of domain II are conserved in OpDHs and are present in AlaDHAm, stucture comparisons, overview
metabolism
physiological function
additional information
metabolism
AlaDHAm is a member of the family of opine dehydrogenases (OpDHs), which catalyze the reductive condensation of pyruvate with an L-amino acid in the presence of NADH to so-called opines during anaerobic glycolysis
metabolism
-
bivalves have evolved diverse and highly specialised strategies for surviving in hypoxic episodes including pathways that are efficient both in terms of ATP production, and in minimising H+ and toxic end product accumulation. Under these circumstances, glycogen is metabolized to pyruvate and the cytosolic NADH/NAD+ redox ratio is balanced by the reduction of pyruvate to lactate. Alternatively, NAD+ can be recycled more efficiently by coupling an amino acid to pyruvate, with formation of opines such as alanopine, tauropine, octopine, and strombine. Specimens utilizing the octopine rather than the alanopine pathway will increase energy flow rapidly, developing a major ability to counteract environmental variations. The high ratio between malate dehydrogenase/lactate dehydrogenase is due to the ability of Pinna nobilis to turn on anaerobic metabolism as a consequence of environmental or anthropogenic stresses. Anaerobic pathways are not all equivalent in terms of energy production based upon maximum rates for ATP output (lactate > octopine > alanopine = strombine)
metabolism
-
the enzyme activities of opine dehydrogenases, including alanopine dehydrogenase, are increased during anaerobic metabolism in corals under prolonged oxygen deprivation, due to invasive algal overgrowth and oxygen deprivation of wide-spread distributed Montipora capitata in Kaneohe Bay, Oahu, Hawaii
physiological function
-
enzyme ADH acts as one of the primary and anaerobic metabolic responses pathways during hypoxia. Montipora capitata increasingly relies upon alanopine dehydrogenase, ADH, and strombine dehydrogenase, SDH, for anaerobic catabolism under low-oxygen conditions
physiological function
-
standard metabolic rate and enzymatic activities (malate dehydrogenase, lactate dehydrogexadnase, alanopine dehydrogenase) in snails after a 10-day acclimation period at high salinity. Opine dehydrogenase is measured for anaerobic respiration. Significantly higher mortalities are observed at higher salinities, the strongest effects occur on snails collected at the end of winter, and exposed to 30 psu and 20°C (100% mortality in 3 days). When snails are collected during the spring, 100% mortality is observed after 40 days at 30 psu and 20°C. Standard metabolic rates are significantly lower when snails are exposed to salinities of 25 and 30 psu, even after 10 days of acclimation. Analysis of effects of high salinity, osmotic and thermal shock, determination of enzyme activity and mortality rates of the New Zealand mudsnail under different conditions, overview
additional information
-
comparisons of opine dehydrogenases activities (octopine dehydrogenase, alanopine dehydrogenase, strombine dehydrogenase, and tauropine dehydrogenase) in the adductor muscle, overview. The ODH activity in adductor muscle increases following the marine-brackish gradient, while the one of ADH, SDH and TDH decreases following the same gradient
additional information
-
enzyme ADH activity varies significantly with respect to hypoxia treatment type, treatment duration, and interaction between treatment duration and type. The combinatory effect of oxygen deprivation over time had no significant effect on ADH activity. Importantly, control and tank samples display no significant differences over 3 h, 6 h, 1 day, and 3 day times sets, indicating that bubbling within small chambers has no effect on target enzyme activity
additional information
L-alanine binding region of alanopine dehydrogenase near a distinct helix-link-helix motif predicted by unbiased molecular dynamics simulations of ligand diffusion using a homology model of alanopine dehydrogenase, overview. L-Alanine is accommodated in a pocket mainly formed by residues Y236, V276, W279, Y280, Y284, L294, N301, and Y304 of domain II, five of which are strictly conserved
additional information
-
L-alanine binding region of alanopine dehydrogenase near a distinct helix-link-helix motif predicted by unbiased molecular dynamics simulations of ligand diffusion using a homology model of alanopine dehydrogenase, overview. L-Alanine is accommodated in a pocket mainly formed by residues Y236, V276, W279, Y280, Y284, L294, N301, and Y304 of domain II, five of which are strictly conserved
