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Literature summary extracted from

  • Uda, K.; Abe, K.; Dehara, Y.; Mizobata, K.; Edashige, Y.; Nishimura, R.; Radkov, A.D.; Moe, L.A.
    Triple serine loop region regulates the aspartate racemase activity of the serine/aspartate racemase family (2017), Amino Acids, 49, 1743-1754 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
5.1.1.13 recombinant expression of C-terminally His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21 (DE3) Crassostrea gigas
5.1.1.13 recombinant expression of C-terminally His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21 (DE3) Acropora millepora
5.1.1.13 sequence comparisons and phylogenetic tree of serine and aspartate racemases, recombinant expression of C-terminally His-tagged wild-type enzyme in Escherichia coli strain BL21(DE3) Penaeus monodon
5.1.1.18 gene SRR, sequence comparisons and phylogenetic tree Mus musculus
5.1.1.18 sequence comparisons and phylogenetic tree Crassostrea gigas
5.1.1.18 sequence comparisons and phylogenetic tree Penaeus monodon
5.1.1.18 sequence comparisons and phylogenetic tree Acropora millepora

Protein Variants

EC Number Protein Variants Comment Organism
5.1.1.13 additional information substituting the triple serine loop region in AspRs enhances serine racemization Penaeus monodon
5.1.1.13 additional information substituting the triple serine loop region in AspRs enhances serine racemization Crassostrea gigas
5.1.1.13 additional information substituting the triple serine loop region in AspRs enhances serine racemization Acropora millepora
5.1.1.13 P150S PCR-based site-directed mutagenesis, the mutant shows reduced aspartate and serine racemase activities compared to the wild-type enzyme Acropora millepora
5.1.1.13 S150P/S151P/S152Y PCR-based site-directed mutagenesis, the SSS to PPY mutation of Crassostrea AspR triple serine loop region drastically decreases the specific AspR activity to below 0.04% compared to wild-type, whereas it significantly increases the specific SerR and SDH activities by 6-13fold. The large change in the AspR activity in the mutant enzyme is caused by approximately 400fold decrease in kcat rather than by 22-32fold decrease in Km Crassostrea gigas
5.1.1.13 S151P/S152F PCR-based site-directed mutagenesis, the mutant is inactive as aspartate racemase, but shows serine racemase activity, EC 5.1.1.18 Acropora millepora
5.1.1.18 H150S site-directed mutagenesis, the mutant shows altered substrate specificity and activity compared to the wild-type enzyme Mus musculus
5.1.1.18 H150S/N152S site-directed mutagenesis, the mutant shows altered substrate specificity and activity compared to the wild-type enzyme Mus musculus
5.1.1.18 H150S/P151S site-directed mutagenesis, the mutant shows altered substrate specificity and activity compared to the wild-type enzyme Mus musculus
5.1.1.18 H150S/P151S/F152S site-directed mutagenesis, the mutant shows altered substrate specificity and activity compared to the wild-type enzyme Penaeus monodon
5.1.1.18 H150S/P151S/N152S site-directed mutagenesis, the mutant shows altered substrate specificity and activity compared to the wild-type enzyme Mus musculus
5.1.1.18 additional information introducing the triple serine loop region into SerRs promotes aspartate racemization Mus musculus
5.1.1.18 additional information introducing the triple serine loop region into SerRs promotes aspartate racemization Crassostrea gigas
5.1.1.18 additional information introducing the triple serine loop region into SerRs promotes aspartate racemization Penaeus monodon
5.1.1.18 additional information introducing the triple serine loop region into SerRs promotes aspartate racemization Acropora millepora
5.1.1.18 N152S site-directed mutagenesis, the mutant shows altered substrate specificity and activity compared to the wild-type enzyme Mus musculus
5.1.1.18 P150S/P151S/F152S site-directed mutagenesis, the mutant shows altered substrate specificity and activity compared to the wild-type enzyme Acropora millepora
5.1.1.18 P150S/P151S/Y152S site-directed mutagenesis, the mutant shows altered substrate specificity and activity compared to the wild-type enzyme Crassostrea gigas
5.1.1.18 P151S site-directed mutagenesis, the mutant shows altered substrate specificity and activity compared to the wild-type enzyme Mus musculus
5.1.1.18 P151S/F152S site-directed mutagenesis, the mutant shows altered substrate specificity and activity compared to the wild-type enzyme Acropora millepora
5.1.1.18 P151S/N152S site-directed mutagenesis, the mutant shows altered substrate specificity and activity compared to the wild-type enzyme Mus musculus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
5.1.1.13 additional information
-
additional information kinetics of enzyme AspR with L-Ser and D-Ser as substrates, comparison to the serine racemase enzyme of Penaeus monodon, EC 5.1.1.18, overview Penaeus monodon
5.1.1.13 additional information
-
additional information kinetics of wild-type and mutant enzymes AspR with L-Ser and D-Ser as substrates, comparison to the serine racemase enzyme of Acropora millepora, overview Acropora millepora
5.1.1.13 additional information
-
additional information kinetics of wild-type and mutant enzymes AspR with L-Ser and D-Ser as substrates, comparison to the serine racemase enzyme of Crassostrea gigas, EC 5.1.1.18, overview Crassostrea gigas
5.1.1.13 1.37
-
D-Aspartate recombinant His-tagged wild-type enzyme, pH 8.0, 30°C Acropora millepora
5.1.1.13 3.11
-
L-aspartate recombinant His-tagged wild-type enzyme, pH 8.0, 30°C Acropora millepora
5.1.1.13 3.2
-
L-aspartate recombinant His-tagged mutant P150S, pH 8.0, 30°C Acropora millepora
5.1.1.13 4.55
-
D-Aspartate recombinant His-tagged mutant P150S, pH 8.0, 30°C Acropora millepora
5.1.1.13 4.75
-
L-aspartate recombinant His-tagged wild-type enzyme, pH 8.0, 30°C Crassostrea gigas
5.1.1.13 6.21
-
D-Aspartate recombinant His-tagged wild-type enzyme, pH 8.0, 30°C Crassostrea gigas
5.1.1.13 9.86
-
D-Aspartate recombinant His-tagged wild-type enzyme, pH 8.0, 30°C Penaeus monodon
5.1.1.13 14.9
-
L-aspartate recombinant His-tagged wild-type enzyme, pH 8.0, 30°C Penaeus monodon
5.1.1.13 48.6
-
L-aspartate recombinant His-tagged mutant S150P/S151P/S152Y, pH 8.0, 30°C Crassostrea gigas
5.1.1.13 80.6
-
D-Aspartate recombinant His-tagged mutant S150P/S151P/S152Y, pH 8.0, 30°C Crassostrea gigas
5.1.1.18 additional information
-
additional information Lineweaver-Burk kinetics Mus musculus
5.1.1.18 additional information
-
additional information Lineweaver-Burk kinetics Crassostrea gigas
5.1.1.18 additional information
-
additional information Lineweaver-Burk kinetics Penaeus monodon
5.1.1.18 additional information
-
additional information Lineweaver-Burk kinetics Acropora millepora
5.1.1.18 7.71
-
L-serine pH 8.0, 30°C, recombinant wild-type enzyme Acropora millepora
5.1.1.18 8.48
-
D-serine pH 8.0, 30°C, recombinant wild-type enzyme Acropora millepora
5.1.1.18 12.7
-
D-serine pH 8.0, 30°C, recombinant mutant P150S/P151S/Y152S Crassostrea gigas
5.1.1.18 14.9
-
L-serine pH 8.0, 30°C, recombinant wild-type enzyme Mus musculus
5.1.1.18 15.1
-
L-serine pH 8.0, 30°C, recombinant mutant P150S/P151S/Y152S Crassostrea gigas
5.1.1.18 18
-
L-serine pH 8.0, 30°C, recombinant mutant N152S Mus musculus
5.1.1.18 19.2
-
L-serine pH 8.0, 30°C, recombinant mutant P150S/P151S/F152S Acropora millepora
5.1.1.18 20.9
-
D-serine pH 8.0, 30°C, recombinant wild-type enzyme Mus musculus
5.1.1.18 21.4
-
D-serine pH 8.0, 30°C, recombinant mutant P151S/F152S Acropora millepora
5.1.1.18 21.5
-
L-serine pH 8.0, 30°C, recombinant wild-type enzyme Crassostrea gigas
5.1.1.18 28.9
-
D-serine pH 8.0, 30°C, recombinant mutant P150S/P151S/F152S Acropora millepora
5.1.1.18 28.9
-
D-serine pH 8.0, 30°C, recombinant mutant P151S Mus musculus
5.1.1.18 29.3
-
D-serine pH 8.0, 30°C, recombinant wild-type enzyme Crassostrea gigas
5.1.1.18 30
-
L-serine pH 8.0, 30°C, recombinant mutant P151S Mus musculus
5.1.1.18 37.4
-
D-serine pH 8.0, 30°C, recombinant mutant H150S Mus musculus
5.1.1.18 38.1
-
L-serine pH 8.0, 30°C, recombinant mutant P151S/N152S Mus musculus
5.1.1.18 42.4
-
L-serine pH 8.0, 30°C, recombinant mutant H150S Mus musculus
5.1.1.18 42.6
-
L-serine pH 8.0, 30°C, recombinant mutant P151S/F152S Acropora millepora
5.1.1.18 44.1
-
D-serine pH 8.0, 30°C, recombinant mutant H150S/P151S Mus musculus
5.1.1.18 45.1
-
D-serine pH 8.0, 30°C, recombinant mutant N152S Mus musculus
5.1.1.18 50.6
-
L-serine pH 8.0, 30°C, recombinant mutant H150S/P151S Mus musculus
5.1.1.18 53.4
-
L-serine pH 8.0, 30°C, recombinant mutant H150S/P151S/N152S Mus musculus
5.1.1.18 55.2
-
D-serine pH 8.0, 30°C, recombinant mutant H150S/N152S Mus musculus
5.1.1.18 69.7
-
D-serine pH 8.0, 30°C, recombinant mutant P151S/N152S Mus musculus
5.1.1.18 69.9
-
L-serine pH 8.0, 30°C, recombinant mutant H150S/N152S Mus musculus
5.1.1.18 119
-
D-serine pH 8.0, 30°C, recombinant wild-type enzyme Penaeus monodon
5.1.1.18 125
-
L-serine pH 8.0, 30°C, recombinant mutant H150S/P151S/F152S Penaeus monodon
5.1.1.18 146
-
L-serine pH 8.0, 30°C, recombinant wild-type enzyme Penaeus monodon
5.1.1.18 172
-
D-serine pH 8.0, 30°C, recombinant mutant H150S/P151S/N152S Mus musculus
5.1.1.18 252
-
D-serine pH 8.0, 30°C, recombinant mutant H150S/P151S/F152S Penaeus monodon

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
5.1.1.13 L-aspartate Penaeus monodon
-
D-aspartate
-
r
5.1.1.13 L-aspartate Crassostrea gigas
-
D-aspartate
-
r
5.1.1.13 L-aspartate Acropora millepora
-
D-aspartate
-
r
5.1.1.13 additional information Penaeus monodon the enzyme AspR also shows low serine racemase, SerR (EC 5.1.1.18), activity ?
-
?
5.1.1.18 L-serine Mus musculus
-
D-serine
-
r
5.1.1.18 L-serine Crassostrea gigas
-
D-serine
-
r
5.1.1.18 L-serine Penaeus monodon
-
D-serine
-
r
5.1.1.18 L-serine Acropora millepora
-
D-serine
-
r

Organism

EC Number Organism UniProt Comment Textmining
5.1.1.13 Acropora millepora JT020910
-
-
5.1.1.13 Crassostrea gigas K1QH67
-
-
5.1.1.13 Penaeus monodon A0A0U5A554
-
-
5.1.1.18 Acropora millepora
-
-
-
5.1.1.18 Crassostrea gigas A0A0U5AKI6
-
-
5.1.1.18 Mus musculus Q9QZX7
-
-
5.1.1.18 Penaeus monodon A0A0U4MRI4
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
5.1.1.13 recombinant C-terminally His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21 (DE3) by nickel affinity chromatography Crassostrea gigas
5.1.1.13 recombinant C-terminally His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21 (DE3) by nickel affinity chromatography Acropora millepora
5.1.1.13 recombinant C-terminally His-tagged wild-type enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography Penaeus monodon

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.1.1.13 D-aspartate
-
Penaeus monodon L-aspartate
-
r
5.1.1.13 D-aspartate
-
Crassostrea gigas L-aspartate
-
r
5.1.1.13 D-aspartate
-
Acropora millepora L-aspartate
-
r
5.1.1.13 L-aspartate
-
Penaeus monodon D-aspartate
-
r
5.1.1.13 L-aspartate
-
Crassostrea gigas D-aspartate
-
r
5.1.1.13 L-aspartate
-
Acropora millepora D-aspartate
-
r
5.1.1.13 additional information the enzyme AspR also shows low serine racemase, SerR (EC 5.1.1.18), activity Penaeus monodon ?
-
?
5.1.1.13 additional information the enzyme AspR also shows negligible serine racemase, SerR (EC 5.1.1.18), activity Crassostrea gigas ?
-
?
5.1.1.13 additional information the enzyme is also active in the racemisation of L- and D-serine, EC 5.1.1.18 Penaeus monodon ?
-
?
5.1.1.18 L-serine
-
Mus musculus D-serine
-
r
5.1.1.18 L-serine
-
Crassostrea gigas D-serine
-
r
5.1.1.18 L-serine
-
Penaeus monodon D-serine
-
r
5.1.1.18 L-serine
-
Acropora millepora D-serine
-
r

Synonyms

EC Number Synonyms Comment Organism
5.1.1.13 AspR
-
Penaeus monodon
5.1.1.13 AspR
-
Crassostrea gigas
5.1.1.13 AspR
-
Acropora millepora
5.1.1.18 SerR
-
Mus musculus
5.1.1.18 SerR
-
Crassostrea gigas
5.1.1.18 SerR
-
Penaeus monodon
5.1.1.18 SerR
-
Acropora millepora
5.1.1.18 SRR
-
Mus musculus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
5.1.1.13 30
-
assay at Penaeus monodon
5.1.1.13 30
-
assay at Crassostrea gigas
5.1.1.13 30
-
assay at Acropora millepora
5.1.1.18
-
-
assay at Penaeus monodon
5.1.1.18 30
-
assay at Mus musculus
5.1.1.18 30
-
assay at Crassostrea gigas
5.1.1.18 30
-
assay at Acropora millepora

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
5.1.1.13 0.0228
-
L-aspartate recombinant His-tagged mutant S150P/S151P/S152Y, pH 8.0, 30°C Crassostrea gigas
5.1.1.13 0.0322
-
D-Aspartate recombinant His-tagged mutant S150P/S151P/S152Y, pH 8.0, 30°C Crassostrea gigas
5.1.1.13 8.65
-
L-aspartate recombinant His-tagged wild-type enzyme, pH 8.0, 30°C Crassostrea gigas
5.1.1.13 13.1
-
D-Aspartate recombinant His-tagged wild-type enzyme, pH 8.0, 30°C Crassostrea gigas
5.1.1.13 14.5
-
L-aspartate recombinant His-tagged mutant P150S, pH 8.0, 30°C Acropora millepora
5.1.1.13 17.8
-
D-Aspartate recombinant His-tagged mutant P150S, pH 8.0, 30°C Acropora millepora
5.1.1.13 25.3
-
D-Aspartate recombinant His-tagged wild-type enzyme, pH 8.0, 30°C Acropora millepora
5.1.1.13 27.6
-
D-Aspartate recombinant His-tagged wild-type enzyme, pH 8.0, 30°C Penaeus monodon
5.1.1.13 33
-
L-aspartate recombinant His-tagged wild-type enzyme, pH 8.0, 30°C Penaeus monodon
5.1.1.13 57.7
-
L-aspartate recombinant His-tagged wild-type enzyme, pH 8.0, 30°C Acropora millepora
5.1.1.18 0.00178
-
L-serine pH 8.0, 30°C, recombinant wild-type enzyme Crassostrea gigas
5.1.1.18 0.00211
-
D-serine pH 8.0, 30°C, recombinant wild-type enzyme Crassostrea gigas
5.1.1.18 0.00264
-
L-serine pH 8.0, 30°C, recombinant mutant P150S/P151S/F152S Acropora millepora
5.1.1.18 0.00366
-
D-serine pH 8.0, 30°C, recombinant mutant P151S/F152S Acropora millepora
5.1.1.18 0.00392
-
D-serine pH 8.0, 30°C, recombinant mutant P150S/P151S/F152S Acropora millepora
5.1.1.18 0.00423
-
D-serine pH 8.0, 30°C, recombinant mutant P150S/P151S/Y152S Crassostrea gigas
5.1.1.18 0.00488
-
L-serine pH 8.0, 30°C, recombinant mutant P150S/P151S/Y152S Crassostrea gigas
5.1.1.18 0.00772
-
D-serine pH 8.0, 30°C, recombinant wild-type enzyme Penaeus monodon
5.1.1.18 0.00861
-
L-serine pH 8.0, 30°C, recombinant mutant P151S/F152S Acropora millepora
5.1.1.18 0.00871
-
L-serine pH 8.0, 30°C, recombinant wild-type enzyme Penaeus monodon
5.1.1.18 0.0335
-
L-serine pH 8.0, 30°C, recombinant mutant H150S/P151S/F152S Penaeus monodon
5.1.1.18 0.0414
-
L-serine pH 8.0, 30°C, recombinant wild-type enzyme Acropora millepora
5.1.1.18 0.0551
-
D-serine pH 8.0, 30°C, recombinant wild-type enzyme Acropora millepora
5.1.1.18 0.057
-
D-serine pH 8.0, 30°C, recombinant mutant H150S/P151S/F152S Penaeus monodon
5.1.1.18 0.277
-
L-serine pH 8.0, 30°C, recombinant mutant H150S/P151S/N152S Mus musculus
5.1.1.18 0.285
-
D-serine pH 8.0, 30°C, recombinant wild-type enzyme Mus musculus
5.1.1.18 0.376
-
D-serine pH 8.0, 30°C, recombinant mutant H150S/P151S Mus musculus
5.1.1.18 0.502
-
L-serine pH 8.0, 30°C, recombinant mutant H150S/P151S Mus musculus
5.1.1.18 0.516
-
D-serine pH 8.0, 30°C, recombinant mutant H150S Mus musculus
5.1.1.18 0.523
-
D-serine pH 8.0, 30°C, recombinant mutant P151S/N152S Mus musculus
5.1.1.18 0.605
-
L-serine pH 8.0, 30°C, recombinant mutant H150S Mus musculus
5.1.1.18 0.611
-
D-serine pH 8.0, 30°C, recombinant mutant H150S/N152S Mus musculus
5.1.1.18 0.816
-
D-serine pH 8.0, 30°C, recombinant mutant H150S/P151S/N152S Mus musculus
5.1.1.18 0.824
-
L-serine pH 8.0, 30°C, recombinant mutant H150S/N152S Mus musculus
5.1.1.18 0.84
-
L-serine pH 8.0, 30°C, recombinant wild-type enzyme Mus musculus
5.1.1.18 0.872
-
L-serine pH 8.0, 30°C, recombinant mutant N152S Mus musculus
5.1.1.18 2.16
-
D-serine pH 8.0, 30°C, recombinant mutant N152S Mus musculus
5.1.1.18 3.74
-
L-serine pH 8.0, 30°C, recombinant mutant P151S/N152S Mus musculus
5.1.1.18 5.68
-
D-serine pH 8.0, 30°C, recombinant mutant P151S Mus musculus
5.1.1.18 5.71
-
L-serine pH 8.0, 30°C, recombinant mutant P151S Mus musculus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
5.1.1.13 8
-
assay at Penaeus monodon
5.1.1.13 8
-
assay at Crassostrea gigas
5.1.1.13 8
-
assay at Acropora millepora
5.1.1.18 8
-
assay at Mus musculus
5.1.1.18 8
-
assay at Crassostrea gigas
5.1.1.18 8
-
assay at Penaeus monodon
5.1.1.18 8
-
assay at Acropora millepora

Cofactor

EC Number Cofactor Comment Organism Structure
5.1.1.18 pyridoxal 5'-phosphate
-
Mus musculus
5.1.1.18 pyridoxal 5'-phosphate
-
Crassostrea gigas
5.1.1.18 pyridoxal 5'-phosphate
-
Penaeus monodon
5.1.1.18 pyridoxal 5'-phosphate
-
Acropora millepora

General Information

EC Number General Information Comment Organism
5.1.1.13 evolution the enzyme belongs to the serine/aspartate racemase family, the triple serine loop region regulates the aspartate racemase activity of the serine/aspartate racemase family members. The ancestral gene of the serine/aspartate racemase family is SerR, the evolution of AspR from SerR occured in three steps: first, gene duplication of the original SerR gene. Second, introduction of the two serine residues at position 151 and 152, resulting in a drastic increase of the AspR activity, and third, formation of the complete triple serine loop region by additional introduction of serine residue at position 150, resulting in enhanced the enzyme specificity for aspartate Penaeus monodon
5.1.1.13 evolution the enzyme belongs to the serine/aspartate racemase family, the triple serine loop region regulates the aspartate racemase activity of the serine/aspartate racemase family members. The ancestral gene of the serine/aspartate racemase family is SerR, the evolution of AspR from SerR occured in three steps: first, gene duplication of the original SerR gene. Second, introduction of the two serine residues at position 151 and 152, resulting in a drastic increase of the AspR activity, and third, formation of the complete triple serine loop region by additional introduction of serine residue at position 150, resulting in enhanced the enzyme specificity for aspartate Crassostrea gigas
5.1.1.13 evolution the enzyme belongs to the serine/aspartate racemase family, the triple serine loop region regulates the aspartate racemase activity of the serine/aspartate racemase family members. The ancestral gene of the serine/aspartate racemase family is SerR, the evolution of AspR from SerR occured in three steps: first, gene duplication of the original SerR gene. Second, introduction of the two serine residues at position 151 and 152, resulting in a drastic increase of the AspR activity, and third, formation of the complete triple serine loop region by additional introduction of serine residue at position 150, resulting in enhanced the enzyme specificity for aspartate Acropora millepora
5.1.1.13 malfunction substituting the triple serine loop region in AspRs enhances serine racemization Penaeus monodon
5.1.1.13 malfunction substituting the triple serine loop region in AspRs enhances serine racemization. Single amino acid substitution mutants, H150S, P151S and N152S, reveal several effects on activity. The Ser150 substitution decreases all enzyme activities, especially the serine dehydrogenase (SDH) activity, while Ser151 dramatically increases the SerR and AspR activities with no change on SDH activity. An increase in the AspR activity is observed after introducing Ser152, while there is little or no change in the other activities Crassostrea gigas
5.1.1.13 malfunction substituting the triple serine loop region in AspRs enhances serine racemization. Single amino acid substitution mutants, H150S, P151S and N152S, reveal several effects on activity. The Ser150 substitution decreases all enzyme activities, especially the serine dehydrogenase (SDH) activity, while Ser151 dramatically increases the SerR and AspR activities with no change on SDH activity. An increase in the AspR activity is observed after introducing Ser152, while there is little or no change in the other activities Acropora millepora
5.1.1.13 additional information important role of triple serine loop region for the aspratate racemase activity in several SerRs and AspRs, structure-function analysis, overview Penaeus monodon
5.1.1.13 additional information important role of triple serine loop region for the aspratate racemase activity in several SerRs and AspRs, structure-function analysis, overview Crassostrea gigas
5.1.1.13 additional information important role of triple serine loop region for the aspratate racemase activity in several SerRs and AspRs, structure-function analysis, overview Acropora millepora
5.1.1.18 evolution SerRs and AspRs are not separated by their racemase functions and form a serine/aspartate racemase family cluster based on phylogenetic analysis Mus musculus
5.1.1.18 evolution SerRs and AspRs are not separated by their racemase functions and form a serine/aspartate racemase family cluster based on phylogenetic analysis, the organism has two paralogous genes, SerR and AspR. The presence of the triple serine loop region in both AspRs and SerRs leads to greater AspR activity while removing the triple serine loop region results in almost complete loss of AspR activity Crassostrea gigas
5.1.1.18 evolution SerRs and AspRs are not separated by their racemase functions and form a serine/aspartate racemase family cluster based on phylogenetic analysis, the organism has two paralogous genes, SerR and AspR. The presence of the triple serine loop region in both AspRs and SerRs leads to greater AspR activity while removing the triple serine loop region results in almost complete loss of AspR activity Penaeus monodon
5.1.1.18 evolution SerRs and AspRs are not separated by their racemase functions and form a serine/aspartate racemase family cluster based on phylogenetic analysis, the organism has two paralogous genes, SerR and AspR. The presence of the triple serine loop region in both AspRs and SerRs leads to greater AspR activity while removing the triple serine loop region results in almost complete loss of AspR activity Acropora millepora
5.1.1.18 additional information role of individual residues at position 150-152, overview Mus musculus
5.1.1.18 additional information role of individual residues at position 150-152, overview Crassostrea gigas
5.1.1.18 additional information role of individual residues at position 150-152, overview Penaeus monodon
5.1.1.18 additional information role of individual residues at position 150-152, overview Acropora millepora

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
5.1.1.13 0.0004
-
D-Aspartate recombinant His-tagged mutant S150P/S151P/S152Y, pH 8.0, 30°C Crassostrea gigas
5.1.1.13 0.0005
-
L-aspartate recombinant His-tagged mutant S150P/S151P/S152Y, pH 8.0, 30°C Crassostrea gigas
5.1.1.13 1.82
-
L-aspartate recombinant His-tagged wild-type enzyme, pH 8.0, 30°C Crassostrea gigas
5.1.1.13 2.12
-
D-Aspartate recombinant His-tagged wild-type enzyme, pH 8.0, 30°C Crassostrea gigas
5.1.1.13 2.22
-
L-aspartate recombinant His-tagged wild-type enzyme, pH 8.0, 30°C Penaeus monodon
5.1.1.13 2.8
-
D-Aspartate recombinant His-tagged wild-type enzyme, pH 8.0, 30°C Penaeus monodon
5.1.1.13 3.9
-
D-Aspartate recombinant His-tagged mutant P150S, pH 8.0, 30°C Acropora millepora
5.1.1.13 4.7
-
L-aspartate recombinant His-tagged mutant P150S, pH 8.0, 30°C Acropora millepora
5.1.1.13 18.4
-
D-Aspartate recombinant His-tagged wild-type enzyme, pH 8.0, 30°C Acropora millepora
5.1.1.13 18.7
-
L-aspartate recombinant His-tagged wild-type enzyme, pH 8.0, 30°C Acropora millepora
5.1.1.18 0.0000559
-
L-serine pH 8.0, 30°C, recombinant wild-type enzyme Penaeus monodon
5.1.1.18 0.0000651
-
D-serine pH 8.0, 30°C, recombinant wild-type enzyme Penaeus monodon
5.1.1.18 0.000137
-
D-serine pH 8.0, 30°C, recombinant mutant P150S/P151S/F152S Acropora millepora
5.1.1.18 0.000138
-
L-serine pH 8.0, 30°C, recombinant mutant P150S/P151S/F152S Acropora millepora
5.1.1.18 0.000174
-
D-serine pH 8.0, 30°C, recombinant mutant P151S/F152S Acropora millepora
5.1.1.18 0.000205
-
L-serine pH 8.0, 30°C, recombinant mutant P151S/F152S Acropora millepora
5.1.1.18 0.000324
-
L-serine pH 8.0, 30°C, recombinant mutant P150S/P151S/Y152S Crassostrea gigas
5.1.1.18 0.000338
-
D-serine pH 8.0, 30°C, recombinant mutant P150S/P151S/Y152S Crassostrea gigas
5.1.1.18 0.000728
-
D-serine pH 8.0, 30°C, recombinant wild-type enzyme Crassostrea gigas
5.1.1.18 0.000827
-
L-serine pH 8.0, 30°C, recombinant wild-type enzyme Crassostrea gigas
5.1.1.18 0.00477
-
D-serine pH 8.0, 30°C, recombinant mutant H150S/P151S/N152S Mus musculus
5.1.1.18 0.00518
-
L-serine pH 8.0, 30°C, recombinant mutant H150S/P151S/N152S Mus musculus
5.1.1.18 0.00538
-
L-serine pH 8.0, 30°C, recombinant wild-type enzyme Acropora millepora
5.1.1.18 0.0065
-
D-serine pH 8.0, 30°C, recombinant wild-type enzyme Acropora millepora
5.1.1.18 0.00858
-
D-serine pH 8.0, 30°C, recombinant mutant H150S/P151S Mus musculus
5.1.1.18 0.00992
-
L-serine pH 8.0, 30°C, recombinant mutant H150S/P151S Mus musculus
5.1.1.18 0.0116
-
D-serine pH 8.0, 30°C, recombinant mutant H150S/N152S Mus musculus
5.1.1.18 0.012
-
L-serine pH 8.0, 30°C, recombinant mutant H150S/N152S Mus musculus
5.1.1.18 0.0132
-
L-serine pH 8.0, 30°C, recombinant mutant H150S Mus musculus
5.1.1.18 0.0141
-
D-serine pH 8.0, 30°C, recombinant mutant H150S Mus musculus
5.1.1.18 0.0402
-
D-serine pH 8.0, 30°C, recombinant wild-type enzyme Mus musculus
5.1.1.18 0.0447
-
L-serine pH 8.0, 30°C, recombinant wild-type enzyme Mus musculus
5.1.1.18 0.0478
-
D-serine pH 8.0, 30°C, recombinant mutant N152S Mus musculus
5.1.1.18 0.0484
-
L-serine pH 8.0, 30°C, recombinant mutant N152S Mus musculus
5.1.1.18 0.0495
-
L-serine pH 8.0, 30°C, recombinant mutant P151S/N152S Mus musculus
5.1.1.18 0.0537
-
D-serine pH 8.0, 30°C, recombinant mutant P151S/N152S Mus musculus
5.1.1.18 0.191
-
L-serine pH 8.0, 30°C, recombinant mutant P151S Mus musculus
5.1.1.18 0.195
-
D-serine pH 8.0, 30°C, recombinant mutant P151S Mus musculus
5.1.1.18 0.226
-
D-serine pH 8.0, 30°C, recombinant mutant H150S/P151S/F152S Penaeus monodon
5.1.1.18 0.268
-
L-serine pH 8.0, 30°C, recombinant mutant H150S/P151S/F152S Penaeus monodon