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Information on EC 1.4.1.1 - alanine dehydrogenase and Organism(s) Archaeoglobus fulgidus and UniProt Accession O28608

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EC Tree
     1 Oxidoreductases
         1.4 Acting on the CH-NH2 group of donors
             1.4.1 With NAD+ or NADP+ as acceptor
                1.4.1.1 alanine dehydrogenase
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Select one or more organisms in this record: ?
This record set is specific for:
Archaeoglobus fulgidus
UNIPROT: O28608 not found.
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Word Map
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  • 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
The taxonomic range for the selected organisms is: Archaeoglobus fulgidus
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
hide
L-alanine
+
H2O
+
NAD+
=
pyruvate
+
NH3
+
NADH
+
H+
+
+
=
+
+
+
Synonyms
scald, alanine dehydrogenase, l-alanine dehydrogenase, 40 kda antigen, l-aladh, shealadh, af1665, (s)alanine dehydrogenase, rv2780, haadh1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
L-Ala dehydrogenase
-
(S)alanine dehydrogenase
-
-
-
-
(S)alanine:NAD oxidoreductase
-
-
-
-
40 kDa antigen
-
-
-
-
ALADH
alanine oxidoreductase
-
-
-
-
alpha-alanine dehydrogenase
-
-
-
-
dehydrogenase, alanine
-
-
-
-
L-alanine dehydrogenase
-
-
-
-
NAD-dependent alanine dehydrogenase
-
-
-
-
NAD-linked alanine dehydrogenase
-
-
-
-
NADH-dependent alanine dehydrogenase
-
-
-
-
TB43
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
oxidative deamination
-
-
-
-
reductive amination
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
L-alanine:NAD+ oxidoreductase (deaminating)
-
CAS REGISTRY NUMBER
COMMENTARY hide
9029-06-5
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-ketocaproate + NH3 + NADH
2-aminocaproate + H2O + NAD+
show the reaction diagram
-
-
-
-
?
3-fluoropyruvate + NH3 + NADH
? + H2O + NAD+
show the reaction diagram
-
-
-
-
?
ketovalerate + NH3 + NADH
2-aminovalerate + H2O + NAD+
show the reaction diagram
-
-
-
-
?
L-2-aminobutyrate + H2O + NAD+
2-oxobutyrate + NH3 + NADH
show the reaction diagram
-
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
show the reaction diagram
L-Asp + H2O + NAD+
oxaloacetate + NH3 + NADH
show the reaction diagram
-
-
-
-
r
L-Ile + H2O + NAD+
2-oxo-3-methylpentanoate + NH3 + NADH
show the reaction diagram
-
-
-
-
?
L-Ser + H2O + NAD+
3-hydroxypyruvate + NH3 + NADH
show the reaction diagram
-
-
-
-
r
L-Thr + H2O + NAD+
3-hydroxy-2-oxobutyrate + NH3 + NADH
show the reaction diagram
-
-
-
-
?
L-Val + H2O + NAD+
3-methyl-2-oxobutanoate + NH3 + NADH
show the reaction diagram
-
-
-
-
?
phenylpyruvate + NH3 + NADH
L-phenylalanine + H2O + NAD+
show the reaction diagram
-
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ketobutyrate
-
-
L-2-aminobutyrate
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.48
2-oxobutyrate
-
pH 8.5, 82°C
0.085
L-2-aminobutyrate
-
pH 8.5, 82°C
0.71
L-Ala
-
pH 8.5, 82°C
0.6
NAD+
-
pH 8.5, 82°C
0.02
NADH
-
pH 8.5, 82°C
17.3
NH4+
-
pH 8.5, 82°C
0.97
oxaloacetate
-
pH 8.5, 82°C
0.16
pyruvate
-
pH 8.5, 82°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
143
2-oxobutyrate
-
pH 8.5, 82°C
9.6
L-2-aminobutyrate
-
pH 8.5, 82°C
6.1
L-Ala
-
pH 8.5, 82°C
6.1
NAD+
-
pH 8.5, 82°C
118
NADH
-
pH 8.5, 82°C
118
NH4+
-
pH 8.5, 82°C
113
oxaloacetate
-
pH 8.5, 82°C
118
pyruvate
-
pH 8.5, 82°C
additional information
additional information
-
-
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4.8
2-Ketobutyrate
-
pH 8.5, 82°C
4.7
L-2-aminobutyrate
-
pH 8.5, 82°C
16.8
L-Ala
-
pH 8.5, 82°C
0.12
NADH
-
pH 8.5, 82°C
27.8
pyruvate
-
pH 8.5, 82°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.4 - 7.4
-
oxidative deamination
7.5
-
reductive amination
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.1 - 8.3
-
pH 6.1: about 60% of maximal activity, pH 8.3: about 60% of maximal activity, reductive amination
6.2 - 8
-
pH 6.2: about 50% of maximal activity, pH 8.0: about 70% of maximal activity, oxidative deamination
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.9
-
calculation from nucleotide sequence
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35000
-
2 * 35000, SDS-PAGE
76000
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
2 * 35000, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of the NAD-bound enzyme at 2.3 A in a C2 crystal form with the 70000 Da dimer in the asymmetric unit
structure of the NAD+-bound AF1665 AlaDH at 2.3 A in a C2 crystal form with the 70000 Da dimer as the asymmetric unit
hanging-drop vapour diffusion method. Crystallized in several forms. One polymorph growing in space group P2(1)2(1)2(1) has non-crystallographic symmetry that becomes crystallographic, changing the space group to P2(1)2(1)2(1) upon binding iridium or samarium
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
-
139 h, no loss of activity
25
-
in presence of 1.5 M KCl stable for 3 months
60
-
less than 5% loss of activity after 65 h
90
-
half-life: 55 h in presence of 1.5 M Kcl
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
optimal KCl concentration for stability is 1.5 M
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
-
batch synthesis of L-Ala at room temperature via reductive amination of pyruvate
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Vadas, A.J.; Schroder, I.; Monbouquette, H.G.
Room-temperature synthesis of L-alanine using the alanine dehydrogenase of the hyperthermophilic archaeon archaeoglobusfulgidus
Biotechnol. Prog.
18
909-911
2002
Archaeoglobus fulgidus
Manually annotated by BRENDA team
Smith, N.; Mayhew, M.; Robinson, H.; Heroux, A.; Charlton, D.; Holden, M.J.; Gallagher, D.T.
Crystallization and phasing of alanine dehydrogenase from Archaeoglobus fulgidus
Acta Crystallogr. Sect. D
59
2328-2331
2003
Archaeoglobus fulgidus
Manually annotated by BRENDA team
Schrder, I.; Vadas, A.; Johnson, E.; Lim, S.; Monbouquette, H.G.
A novel archaeal alanine dehydrogenase homologous to ornithine cyclodeaminase and mu-crystallin
J. Bacteriol.
186
7680-7689
2004
Archaeoglobus fulgidus
Manually annotated by BRENDA team
Gallagher, D.T.; Monbouquette, H.G.; Schroder, I.; Robinson, H.; Holden, M.J.; Smith, N.N.
Structure of alanine dehydrogenase from Archaeoglobus: active site analysis and relation to bacterial cyclodeaminases and mammalian mu crystallin
J. Mol. Biol.
342
119-130
2004
Archaeoglobus fulgidus (O28608), Archaeoglobus fulgidus
Manually annotated by BRENDA team