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Literature summary for 5.1.1.13 extracted from

  • Katane, M.; Nakayama, K.; Kawata, T.; Yokoyama, Y.; Matsui, Y.; Kaneko, Y.; Matsuda, S.; Saitoh, Y.; Miyamoto, T.; Sekine, M.; Homma, H.
    A sensitive assay for measuring aspartate-specific amino acid racemase activity (2015), J. Pharm. Biomed. Anal., 116, 109-115 .
    View publication on PubMed
Search for more literature for 5.1.1.13

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)pLysS Streptococcus thermophilus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information steady-state kinetics of all assay methods, overview Streptococcus thermophilus
6.37
-
 L-aspartate recombinant enzyme, pH 8.3, 37°C, coupling method assay Streptococcus thermophilus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-aspartate Streptococcus thermophilus
-
 D-aspartate
-
 r

Organism

Organism UniProt Comment Textmining
Streptococcus thermophilus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3)pLysS by nickel affinity chromatography Streptococcus thermophilus

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
19.5
-
 crude recombinant enzyme in Escherichia coli cell extract, coupled assay method, pH 8.3, 37°C Streptococcus thermophilus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-aspartate
-
 Streptococcus thermophilus D-aspartate
-
 r
L-aspartate the Asp racemase reaction is reversible, and D- and L-Asp are formed from the corresponding enantiomers in the reaction mixture. In the reaction mixture, the L-Asp substrate initially binds to Asp racemase and D-Asp is released from the enzyme as the reaction product Streptococcus thermophilus D-aspartate
-
 r
additional information development of a sensitive assay method for measuring aspartate-specific amino acid racemase activity using recombinant Streptococcus thermophilus Asp racemase as a model enzyme. The coupling method (using D-Asp oxidase (DDO), a degradative enzyme that stereospecifically acts on D-Asp) is more accurate and sensitive than the other two methods analyzed, and can be used for the determination of Asp racemase activity, overview. DDO is concomitantly included in the Asp racemase reaction mixture, and the Asp racemase reaction is readily coupled to the D-Asp degradative reaction by DDO during the incubation. Human DDO is used to degrade D-Asp formed from L-Asp by the Asp racemase reaction to 2-oxoacid, the amounts of which are determined using a colorimetric assay. Methods evaluation and optimization, overview Streptococcus thermophilus ?
-
 ?

Subunits

Subunits Comment Organism
? x * 27945, sequence calculation Streptococcus thermophilus

Synonyms

Synonyms Comment Organism
Asp racemase
-
 Streptococcus thermophilus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Streptococcus thermophilus

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
39.6
-
 L-aspartate recombinant enzyme, pH 8.3, 37°C, coupling method assay Streptococcus thermophilus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.3
-
 assay at Streptococcus thermophilus

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
6.22
-
 L-aspartate recombinant enzyme, pH 8.3, 37°C, coupling method assay Streptococcus thermophilus