1.4.1.1: alanine dehydrogenase
This is an abbreviated version!
For detailed information about alanine dehydrogenase, go to the full flat file.
Word Map on EC 1.4.1.1
-
1.4.1.1
-
burn
-
children
-
postburn
-
sham
-
full-thickness
-
flame
-
admitted
-
superficial
-
admission
-
resuscitation
-
injured
-
trauma
-
sepsis
-
inflict
-
burn-induced
-
ringer
-
sacrificed
-
third-degree
-
anesthetized
-
immersion
-
xanthomonas
-
barley
-
child
-
demographic
-
dress
-
partial-thickness
-
victim
-
sugarcane
-
accident
-
home
-
second-degree
-
xylella
-
dorsum
-
work-related
-
postinjury
-
thermostat
-
epithelialization
-
debridement
-
hereinafter
-
1-methylcyclopropene
-
biotechnology
-
synthesis
-
fastidiosa
-
heater
-
toddler
-
hypermetabolic
-
delicious
-
guadeloupe
-
kitchen
-
diphenylamine
-
medicine
-
eschar
-
nutrition
-
analysis
-
shower
- 1.4.1.1
-
burn
- children
-
postburn
-
sham
-
full-thickness
-
flame
-
admitted
-
superficial
-
admission
-
resuscitation
-
injured
-
trauma
-
sepsis
-
inflict
-
burn-induced
-
ringer
-
sacrificed
-
third-degree
-
anesthetized
-
immersion
-
xanthomonas
- barley
- child
-
demographic
-
dress
-
partial-thickness
-
victim
-
sugarcane
-
accident
-
home
-
second-degree
-
xylella
-
dorsum
-
work-related
-
postinjury
-
thermostat
-
epithelialization
-
debridement
-
hereinafter
- 1-methylcyclopropene
- biotechnology
- synthesis
-
fastidiosa
-
heater
-
toddler
-
hypermetabolic
-
delicious
-
guadeloupe
-
kitchen
- diphenylamine
- medicine
-
eschar
- nutrition
- analysis
-
shower
Reaction
Synonyms
(S)alanine dehydrogenase, (S)alanine:NAD oxidoreductase, 40 kDa antigen, ADH, AF1665, ALADH, alanine dehydrogenase, alanine oxidative deaminase, alanine oxidoreductase, ALD, AldA, alpha-alanine dehydrogenase, ApalaDH, AsAlaDH, CQA66_00465, dehydrogenase, alanine, glyoxylate reductive aminase, GxrA, HAADH1, HAADH2, L-Ala dehydrogenase, L-AlaDH, L-AlaDH-Bs, L-alanine dehydrogenase, MtbALD, NAD(H)-dependent L-alanine dehydrogenase, NAD+ dependent amino acid dehydrogenase, NAD+-dependent alanine dehydrogenase, NAD-dependent alanine dehydrogenase, NAD-linked alanine dehydrogenase, NADH-dependent alanine dehydrogenase, OF4Ald, PlaAlaDH, PvRA, pyruvate reductive aminase, Rv2780, ScALD, SCO1773, SheAlaDH, TB43
ECTree
1.4.1.1 alanine dehydrogenaseAdvanced search results
results (
results (Engineering
Engineering on EC 1.4.1.1 - alanine dehydrogenase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
top
PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
K73A
Alkalihalophilus pseudofirmus
site-directed mutagenesis, the mutant shows 6fold improvement in kcat/Km towards L-alanine as compared to the wild-type enzyme, the mutant is slightly more temperture-sensitive compared to wild-type
H96A
Alkalihalophilus pseudofirmus ATCC BAA-2126
-
site-directed mutagenesis
-
K73A
Alkalihalophilus pseudofirmus ATCC BAA-2126
-
site-directed mutagenesis, the mutant shows 6fold improvement in kcat/Km towards L-alanine as compared to the wild-type enzyme, the mutant is slightly more temperture-sensitive compared to wild-type
-
K73Q
Alkalihalophilus pseudofirmus ATCC BAA-2126
-
site-directed mutagenesis
-
K75A
Alkalihalophilus pseudofirmus ATCC BAA-2126
-
site-directed mutagenesis
-
H96A
Alkalihalophilus pseudofirmus JCM 17055
-
site-directed mutagenesis
-
K73A
Alkalihalophilus pseudofirmus JCM 17055
-
site-directed mutagenesis, the mutant shows 6fold improvement in kcat/Km towards L-alanine as compared to the wild-type enzyme, the mutant is slightly more temperture-sensitive compared to wild-type
-
K73Q
Alkalihalophilus pseudofirmus JCM 17055
-
site-directed mutagenesis
-
K75A
Alkalihalophilus pseudofirmus JCM 17055
-
site-directed mutagenesis
-
H96A
Alkalihalophilus pseudofirmus OF4
-
site-directed mutagenesis
-
K73A
Alkalihalophilus pseudofirmus OF4
-
site-directed mutagenesis, the mutant shows 6fold improvement in kcat/Km towards L-alanine as compared to the wild-type enzyme, the mutant is slightly more temperture-sensitive compared to wild-type
-
K73Q
Alkalihalophilus pseudofirmus OF4
-
site-directed mutagenesis
-
K75A
Alkalihalophilus pseudofirmus OF4
-
site-directed mutagenesis
-
D196A
-
alterating cofactor specificity from NADH to NADPH, 10fold decrease in activity with NADH, 4fold increase in activity with NADPH
D196A/L197R
-
alterating cofactor specificity from NADH to NADPH, almost the same activity with NADPH as the wild-type enzyme for NADH
D196A/L197R/N198S/R201A
-
alterating cofactor specificity from NADH to NADPH, loss of activity with NADH, 5fold increase in activity with NADPH
D196A/L197R/R201A
-
alterating cofactor specificity from NADH to NADPH, loss of activity with NADH, 2fold increase in activity with NADPH
D270N
D270N/H96A
the protein can still convert its conformation from open state to closed state. The key interactions between NADH and Asn270 disappear with mutation, with loss of protein activity
F94S
mutation alters its substrate specificity pattern, enabling activity toward a range of larger amino acids
F94S/Y117L
mutant shows improved activity toward hydrophobic amino acids
H96A
D270N
-
upon mutation of residue D270 or H96A, the protein always changes its conformations from open state to closed state upon binding NADH. The nicotinamide ring and ribose of NADH is unstable due to the loss of interactions of NADH with Asp270, and the structural rearrangement of active site leads to an orientation change of Asn270 and Gln271, which makes the protein lose its activity
-
D270N/H96A
-
the protein can still convert its conformation from open state to closed state. The key interactions between NADH and Asn270 disappear with mutation, with loss of protein activity
-
F94S
-
mutation alters its substrate specificity pattern, enabling activity toward a range of larger amino acids
-
F94S/Y117L
-
mutant shows improved activity toward hydrophobic amino acids
-
H96A
-
upon mutation of residue D270 or H96A, the protein always changes its conformations from open state to closed state upon binding NADH. The nicotinamide ring and ribose of NADH is unstable due to the loss of interactions of NADH with Asp270, and the structural rearrangement of active site leads to an orientation change of Asn270 and Gln271, which makes the protein lose its activity
-
D198A
-
mutant enzyme shows higher efficiency with NADP+ as coenzyme than with NAD+
D198G
-
mutant enzyme shows higher efficiency with NADP+ as coenzyme than with NAD+
D198L
-
mutant enzyme shows higher efficiency with NADP+ as coenzyme than with NAD+
D198V
-
mutant enzyme shows higher efficiency with NADP+ as coenzyme than with NAD+
D198A
-
mutant enzyme shows higher efficiency with NADP+ as coenzyme than with NAD+
-
D198G
-
mutant enzyme shows higher efficiency with NADP+ as coenzyme than with NAD+
-
D198L
-
mutant enzyme shows higher efficiency with NADP+ as coenzyme than with NAD+
-
D198V
-
mutant enzyme shows higher efficiency with NADP+ as coenzyme than with NAD+
-
additional information
D270N
-
inactive, the bifurcated hydrogen bond between Asp270 and the ribose of NAD is replaced by a single hydrogen bond
D270N
upon mutation of residue D270 or H96A, the protein always changes its conformations from open state to closed state upon binding NADH. The nicotinamide ring and ribose of NADH is unstable due to the loss of interactions of NADH with Asp270, and the structural rearrangement of active site leads to an orientation change of Asn270 and Gln271, which makes the protein lose its activity
H96A
upon mutation of residue D270 or H96A, the protein always changes its conformations from open state to closed state upon binding NADH. The nicotinamide ring and ribose of NADH is unstable due to the loss of interactions of NADH with Asp270, and the structural rearrangement of active site leads to an orientation change of Asn270 and Gln271, which makes the protein lose its activity
additional information
Alkalihalophilus pseudofirmus
mutations at four conserved residue Arg15, Lys75, His-6 and Asp269 (except residue Lys73) result in a complete loss in enzymatic activity, which signifies that these predicted active sites are indispensable for OF4Ald activity
additional information
Alkalihalophilus pseudofirmus ATCC BAA-2126
-
mutations at four conserved residue Arg15, Lys75, His-6 and Asp269 (except residue Lys73) result in a complete loss in enzymatic activity, which signifies that these predicted active sites are indispensable for OF4Ald activity
-
additional information
Alkalihalophilus pseudofirmus JCM 17055
-
mutations at four conserved residue Arg15, Lys75, His-6 and Asp269 (except residue Lys73) result in a complete loss in enzymatic activity, which signifies that these predicted active sites are indispensable for OF4Ald activity
-
additional information
Alkalihalophilus pseudofirmus OF4
-
mutations at four conserved residue Arg15, Lys75, His-6 and Asp269 (except residue Lys73) result in a complete loss in enzymatic activity, which signifies that these predicted active sites are indispensable for OF4Ald activity
-
additional information
-
inactivation of gene ald results in a lack of alanine dehydrogenase activity, a substantially decreased nitrogenase activity, and a 50% reduction in the rate of diazotrophic growth. While production of alanine is not affected in the ald mutant, alanine catabolism is hampered. Construction of several mutant strains, e,g, the insertion mutant strain CSR24, phenotypes, overview
additional information
-
inactivation of gene ald results in a lack of alanine dehydrogenase activity, a substantially decreased nitrogenase activity, and a 50% reduction in the rate of diazotrophic growth. While production of alanine is not affected in the ald mutant, alanine catabolism is hampered. Construction of several mutant strains, e,g, the insertion mutant strain CSR24, phenotypes, overview
-
additional information
biocatalytic deracemization of aliphatic amino acids into D-enantiomers by running cascade reactions: (1) stereoinversion of L-alanine to a D-form by L-alanine dehydrogenase and omega-transaminase and (2) regeneration of NAD+ by NADH oxidase. Under the cascade reaction conditions containing 100 mM isopropylamine and 1 mM NAD+, complete deracemization of 100 mM DL-alanine is achieved after 24 h with 95% reaction yield of D-alanine (over 99% enantiomeric excess, 52% isolation yield). AlaDH produces pyruvate from L-alanine with NAD+, NOX oxidizes NADH to NAD+, and reductive amination of the resulting pyruvate back to the amino acid in an enantiomerically opposite form by D-selective omega-transaminase (omega-TA) using isopropylamine as an amino donor cosubstrate. Method evaluation, overview
additional information
the purified enzyme is immobilized on porous agarose microbeads activated with glyoxyl groups (aliphatic aldehydes). 85% of the offered enzyme is immobilized on these microbeads and the enzyme recovers 45% of its initial reduction amination activity upon the multivalent and irreversible attachment. The immobilized enzyme shows 13fold increased thermostability compared to the soluble enzyme. The optimally immobilized enzyme is also stabilized against acidic pH. The enzyme works as heterogeneous biocatalyst for the synthesis of L-[13N]alanine using pyruvate and [13N]NH4OH obtaining a radiochemical yield of over 95% in 20 minutes. This immobilized enzyme is reused for up to 5 cycles keeping the maximum yield. Immobilization method optimization, overview
additional information
-
biocatalytic deracemization of aliphatic amino acids into D-enantiomers by running cascade reactions: (1) stereoinversion of L-alanine to a D-form by L-alanine dehydrogenase and omega-transaminase and (2) regeneration of NAD+ by NADH oxidase. Under the cascade reaction conditions containing 100 mM isopropylamine and 1 mM NAD+, complete deracemization of 100 mM DL-alanine is achieved after 24 h with 95% reaction yield of D-alanine (over 99% enantiomeric excess, 52% isolation yield). AlaDH produces pyruvate from L-alanine with NAD+, NOX oxidizes NADH to NAD+, and reductive amination of the resulting pyruvate back to the amino acid in an enantiomerically opposite form by D-selective omega-transaminase (omega-TA) using isopropylamine as an amino donor cosubstrate. Method evaluation, overview
-
additional information
-
the purified enzyme is immobilized on porous agarose microbeads activated with glyoxyl groups (aliphatic aldehydes). 85% of the offered enzyme is immobilized on these microbeads and the enzyme recovers 45% of its initial reduction amination activity upon the multivalent and irreversible attachment. The immobilized enzyme shows 13fold increased thermostability compared to the soluble enzyme. The optimally immobilized enzyme is also stabilized against acidic pH. The enzyme works as heterogeneous biocatalyst for the synthesis of L-[13N]alanine using pyruvate and [13N]NH4OH obtaining a radiochemical yield of over 95% in 20 minutes. This immobilized enzyme is reused for up to 5 cycles keeping the maximum yield. Immobilization method optimization, overview
-
additional information
-
coimmobilization of malic enzyme and alanine dehydrogenase on organic-inorganic hybrid gel fibers of cellulose acetate and zirconium alkoxide by air-gap wet spinning, and the production of L-alanine from malic acid using the fibers with coenzyme regeneration, overview
additional information
-
generation of ald knockout strain RVW7 from wild-type strain H37Rv
additional information
-
generation of ald knockout strain RVW7 from wild-type strain H37Rv
-
additional information
generation of a DELTAaldR mutant strain
additional information
-
generation of a DELTAaldR mutant strain
-
additional information
-
generation of a DELTAaldR mutant strain
-
additional information
an enzymatic assay system to eliminate or measure D-Ala, which is reported to affect the taste of seafoods or sake, is constructed using alanine racemase (L-AlaR from Synechocystis sp. PCC6803) and L-alanine dehydrogenase (L-AlaDH from Phormidium lapideum). D-Ala is converted to L-Ala by alanine racemase and then deaminated by L-alanine dehydrogenase with the reduction of NAD+ to NADH, which is determined with water-soluble tetrazolium. NADH nonenzymatically reduces WST-1 to form water soluble formazan. Using the assay system, the D-Ala contents of 7 crustaceans are determined. Method evaluation, overview
additional information
construction of an amperometric biosensor using AlaDH of Streptomyces anulatus amidst the working electrode (3 mm diameter) present at the center of the screen printed electrode. The mixture contains AlaDH (80 mg/ml of freeze dried enzyme), NADH (200 mg/ml), pyruvate (80 mg/ml) and the binder 1% poly HEMA (poly-hydroxyethylmethacrylate) in 50 mM Tris-HCl buffer, pH 8.5. The mixture is allowed to dry at 4°C. The weight of the sensor strip after immobilizing the mixture is 0.56 g sensor strips are incubated at different temperatures (10-70°C) for 5 min before placing the samples (10 mM ammonium chloride dissolved in buffers of different pH) on the strip during the measurement of output current. The output current is measured by cyclic voltammetry by using a potentiostat
additional information
Streptomyces anulatus MTCC 2528
-
construction of an amperometric biosensor using AlaDH of Streptomyces anulatus amidst the working electrode (3 mm diameter) present at the center of the screen printed electrode. The mixture contains AlaDH (80 mg/ml of freeze dried enzyme), NADH (200 mg/ml), pyruvate (80 mg/ml) and the binder 1% poly HEMA (poly-hydroxyethylmethacrylate) in 50 mM Tris-HCl buffer, pH 8.5. The mixture is allowed to dry at 4°C. The weight of the sensor strip after immobilizing the mixture is 0.56 g sensor strips are incubated at different temperatures (10-70°C) for 5 min before placing the samples (10 mM ammonium chloride dissolved in buffers of different pH) on the strip during the measurement of output current. The output current is measured by cyclic voltammetry by using a potentiostat
-
additional information
construction an ald gene deletion strain (SCDELTAALD) by double crossover in-frame deletion of the ald gene (SCO1773) in wild-type strain SCWT by PCR targeting. An ald complementation strain SC-ALD is generated by using a site-specific integrating vector pMS81 that inserts into PhiBT1 attB site of SCDELTAALD. An effect of the ald gene deletion on the pigmentation during sporulation on solid agar medium in observed. Mutant SCDELTAALD spores have a paler appearance compared to the standard brownish gray pigmentation for the wild-type SCWT spores. This reduced pigmentation is complemented, and the standard brownish gray pigmentation reappeares during SC-ALD sporulation
additional information
-
construction an ald gene deletion strain (SCDELTAALD) by double crossover in-frame deletion of the ald gene (SCO1773) in wild-type strain SCWT by PCR targeting. An ald complementation strain SC-ALD is generated by using a site-specific integrating vector pMS81 that inserts into PhiBT1 attB site of SCDELTAALD. An effect of the ald gene deletion on the pigmentation during sporulation on solid agar medium in observed. Mutant SCDELTAALD spores have a paler appearance compared to the standard brownish gray pigmentation for the wild-type SCWT spores. This reduced pigmentation is complemented, and the standard brownish gray pigmentation reappeares during SC-ALD sporulation
additional information
-
construction an ald gene deletion strain (SCDELTAALD) by double crossover in-frame deletion of the ald gene (SCO1773) in wild-type strain SCWT by PCR targeting. An ald complementation strain SC-ALD is generated by using a site-specific integrating vector pMS81 that inserts into PhiBT1 attB site of SCDELTAALD. An effect of the ald gene deletion on the pigmentation during sporulation on solid agar medium in observed. Mutant SCDELTAALD spores have a paler appearance compared to the standard brownish gray pigmentation for the wild-type SCWT spores. This reduced pigmentation is complemented, and the standard brownish gray pigmentation reappeares during SC-ALD sporulation
-
additional information
-
construction an ald gene deletion strain (SCDELTAALD) by double crossover in-frame deletion of the ald gene (SCO1773) in wild-type strain SCWT by PCR targeting. An ald complementation strain SC-ALD is generated by using a site-specific integrating vector pMS81 that inserts into PhiBT1 attB site of SCDELTAALD. An effect of the ald gene deletion on the pigmentation during sporulation on solid agar medium in observed. Mutant SCDELTAALD spores have a paler appearance compared to the standard brownish gray pigmentation for the wild-type SCWT spores. This reduced pigmentation is complemented, and the standard brownish gray pigmentation reappeares during SC-ALD sporulation
-
additional information
-
construction an ald gene deletion strain (SCDELTAALD) by double crossover in-frame deletion of the ald gene (SCO1773) in wild-type strain SCWT by PCR targeting. An ald complementation strain SC-ALD is generated by using a site-specific integrating vector pMS81 that inserts into PhiBT1 attB site of SCDELTAALD. An effect of the ald gene deletion on the pigmentation during sporulation on solid agar medium in observed. Mutant SCDELTAALD spores have a paler appearance compared to the standard brownish gray pigmentation for the wild-type SCWT spores. This reduced pigmentation is complemented, and the standard brownish gray pigmentation reappeares during SC-ALD sporulation
-
additional information
-
mutant Aldomega, deficient in transcription induction of a number of genes during nitrogen starvation, transcripts of several specific nitrogen-responsive genes accumulate at lower levels in the mutant than in the wild-type strain, accumulates alanine upon nitrogen starvation, does not decrease the accumulation of transcripts during sulfur starvation, attenuated phycobilisome degradation during nitrogen starvation
