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Literature summary for 1.4.1.21 extracted from

  • Ozyurt, C.; Evran, S.; Telefoncu, A.
    Development of a novel fluorescent protein construct by genetically fusing green fluorescent protein to the N-terminal of aspartate dehydrogenase (2013), Biotechnol. Appl. Biochem., 60, 399-404.
    View publication on PubMed
Search for more literature for 1.4.1.21

Application

Application Comment Organism
analysis development of a genetically encoded fluorescent protein construct for monitoring of L-Asp in vitro, and employment of aspartate dehydrogenase scaffold as a biorecognition element Thermotoga maritima

Cloned(Commentary)

Cloned (Comment) Organism
expression of N-terminally His-tagged and GFP-tagged enzyme, using the flexible GGSGG linker, in Escherichia coli. The recombinant tagged aspartate dehydrogenase functions as the biorecognition element, and aspartate-induced conformational change is converted to a fluorescence signal by GFP, method, overview Thermotoga maritima

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-aspartate + H2O + NAD(P)+ Thermotoga maritima
-
 oxaloacetate + NH3 + NAD(P)H + H+
-
 r

Organism

Organism UniProt Comment Textmining
Thermotoga maritima
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography Thermotoga maritima

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-aspartate + H2O + NAD(P)+
-
 Thermotoga maritima oxaloacetate + NH3 + NAD(P)H + H+
-
 r
additional information high substrate specificity of aspartate dehydrogenase enzyme Thermotoga maritima ?
-
 ?

Cofactor

Cofactor Comment Organism Structure
NAD+
-
 Thermotoga maritima
NADH
-
 Thermotoga maritima
NADP+
-
 Thermotoga maritima
NADPH
-
 Thermotoga maritima