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Literature summary extracted from

  • Kawakami, R.; Sakuraba, H.; Ohmori, T.; Ohshima, T.
    First characterization of an archaeal amino acid racemase with broad substrate specificity from the hyperthermophile Pyrococcus horikoshii OT-3 (2017), J. Biosci. Bioeng., 124, 23-27 .
    View publication on PubMed

Application

EC Number Application Comment Organism
5.1.1.10 synthesis the high reactivity toward Trp and Tyr, as well as extremely high thermostability, is likely a major advantage of using BAR for biochemical conversion of these aromatic amino acids Pyrococcus horikoshii

Cloned(Commentary)

EC Number Cloned (Comment) Organism
5.1.1.10 enzyme is produced mainly as an inclusion body in Escherichia coli. In this study, expression of the recombinant protein into the soluble fraction is markedly improved by coexpression with chaperone molecules Pyrococcus horikoshii
5.1.1.10 recombinant expression of enzyme BAR in inclusion bodies in Escherichia coli strain BL21(DE3), expression of the recombinant protein in the soluble fraction is markedly improved by co-expression with chaperone molecules, i.e. chaperone proteins DnaK-DnaJ-GrpE and GroEL-GroES, GroELGroES and Tig, and Tig, method optimization Pyrococcus horikoshii

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
5.1.1.10 1.68
-
 D-Trp pH 7.0, 80°C Pyrococcus horikoshii
5.1.1.10 1.68
-
 D-tryptophan pH 7.0, 80°C, recombinant enzyme Pyrococcus horikoshii
5.1.1.10 2.23
-
 L-Tyr pH 7.0, 80°C Pyrococcus horikoshii
5.1.1.10 2.23
-
 L-tyrosine pH 7.0, 80°C, recombinant enzyme Pyrococcus horikoshii
5.1.1.10 2.77
-
 D-Tyr pH 7.0, 80°C Pyrococcus horikoshii
5.1.1.10 2.77
-
 D-tyrosine pH 7.0, 80°C, recombinant enzyme Pyrococcus horikoshii
5.1.1.10 2.78
-
 D-Phe pH 7.0, 80°C Pyrococcus horikoshii
5.1.1.10 2.78
-
 D-phenylalanine pH 7.0, 80°C, recombinant enzyme Pyrococcus horikoshii
5.1.1.10 3.41
-
 L-Val pH 7.0, 80°C Pyrococcus horikoshii
5.1.1.10 3.41
-
 L-valine pH 7.0, 80°C, recombinant enzyme Pyrococcus horikoshii
5.1.1.10 3.94
-
 L-Ile pH 7.0, 80°C Pyrococcus horikoshii
5.1.1.10 3.94
-
 L-isoleucine pH 7.0, 80°C, recombinant enzyme Pyrococcus horikoshii
5.1.1.10 4.19
-
 D-Leu pH 7.0, 80°C Pyrococcus horikoshii
5.1.1.10 4.19
-
 D-leucine pH 7.0, 80°C, recombinant enzyme Pyrococcus horikoshii
5.1.1.10 4.28
-
 L-Met pH 7.0, 80°C Pyrococcus horikoshii
5.1.1.10 4.28
-
 L-methionine pH 7.0, 80°C, recombinant enzyme Pyrococcus horikoshii
5.1.1.10 4.95
-
 L-Leu pH 7.0, 80°C Pyrococcus horikoshii
5.1.1.10 4.95
-
 L-leucine pH 7.0, 80°C, recombinant enzyme Pyrococcus horikoshii
5.1.1.10 5.84
-
 L-Trp pH 7.0, 80°C Pyrococcus horikoshii
5.1.1.10 5.84
-
 L-tryptophan pH 7.0, 80°C, recombinant enzyme Pyrococcus horikoshii
5.1.1.10 7.86
-
 D-Met pH 7.0, 80°C Pyrococcus horikoshii
5.1.1.10 7.86
-
 D-methionine pH 7.0, 80°C, recombinant enzyme Pyrococcus horikoshii
5.1.1.10 8.23
-
 L-Phe pH 7.0, 80°C Pyrococcus horikoshii
5.1.1.10 8.23
-
 L-phenylalanine pH 7.0, 80°C, recombinant enzyme Pyrococcus horikoshii
5.1.1.10 9.54
-
 D-Ile pH 7.0, 80°C Pyrococcus horikoshii
5.1.1.10 9.54
-
 D-isoleucine pH 7.0, 80°C, recombinant enzyme Pyrococcus horikoshii
5.1.1.10 9.82
-
 D-Val pH 7.0, 80°C Pyrococcus horikoshii
5.1.1.10 9.82
-
 D-valine pH 7.0, 80°C, recombinant enzyme Pyrococcus horikoshii
5.1.1.10 35.6
-
 D-Ala pH 7.0, 80°C Pyrococcus horikoshii
5.1.1.10 35.6
-
 D-alanine pH 7.0, 80°C, recombinant enzyme Pyrococcus horikoshii
5.1.1.10 56
-
 L-Ala pH 7.0, 80°C Pyrococcus horikoshii
5.1.1.10 56
-
 L-alanine pH 7.0, 80°C, recombinant enzyme Pyrococcus horikoshii

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
5.1.1.10 91000
-
 gel filtration Pyrococcus horikoshii
5.1.1.10 91000
-
 recombinant enzyme, gel filtration Pyrococcus horikoshii

Organism

EC Number Organism UniProt Comment Textmining
5.1.1.10 Pyrococcus horikoshii O57878
-
-
5.1.1.10 Pyrococcus horikoshii OT-3 O57878
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
5.1.1.10
-
 Pyrococcus horikoshii
5.1.1.10 recombinant soluble enzyme BAR from Escherichia coli strain BL21(DE3) by heat treatment at 90°C for 20 min, ammonium sulfate fractionation, and hydrophobic interaction chromatography, dialysis, anion echange chromatography, and again dialysis Pyrococcus horikoshii

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.1.1.10 D-Ala
-
 Pyrococcus horikoshii L-Ala
-
 r
5.1.1.10 D-alanine
-
 Pyrococcus horikoshii L-alanine
-
 r
5.1.1.10 D-Ile
-
 Pyrococcus horikoshii L-Ile
-
 r
5.1.1.10 D-isoleucine
-
 Pyrococcus horikoshii L-isoleucine
-
 r
5.1.1.10 D-Leu
-
 Pyrococcus horikoshii L-Leu
-
 r
5.1.1.10 D-leucine
-
 Pyrococcus horikoshii L-leucine
-
 r
5.1.1.10 D-Met
-
 Pyrococcus horikoshii L-Met
-
 r
5.1.1.10 D-methionine
-
 Pyrococcus horikoshii L-methionine
-
 r
5.1.1.10 D-Phe
-
 Pyrococcus horikoshii L-Phe
-
 r
5.1.1.10 D-phenylalanine
-
 Pyrococcus horikoshii L-phenylalanine
-
 r
5.1.1.10 D-serine
-
 Pyrococcus horikoshii L-serine
-
 r
5.1.1.10 D-threonine
-
 Pyrococcus horikoshii L-threonine
-
 r
5.1.1.10 D-Trp
-
 Pyrococcus horikoshii L-Trp
-
 r
5.1.1.10 D-tryptophan
-
 Pyrococcus horikoshii L-tryptophan
-
 r
5.1.1.10 D-Tyr
-
 Pyrococcus horikoshii L-Tyr
-
 r
5.1.1.10 D-tyrosine
-
 Pyrococcus horikoshii L-tyrosine
-
 r
5.1.1.10 D-Val
-
 Pyrococcus horikoshii L-Val
-
 r
5.1.1.10 D-valine
-
 Pyrococcus horikoshii L-valine
-
 r
5.1.1.10 L-Ala
-
 Pyrococcus horikoshii D-Ala
-
 r
5.1.1.10 L-Ala
-
 Pyrococcus horikoshii OT-3 D-Ala
-
 r
5.1.1.10 L-alanine
-
 Pyrococcus horikoshii D-alanine
-
 r
5.1.1.10 L-Ile
-
 Pyrococcus horikoshii D-Ile
-
 r
5.1.1.10 L-isoleucine
-
 Pyrococcus horikoshii D-isoleucine
-
 r
5.1.1.10 L-Leu
-
 Pyrococcus horikoshii D-Leu
-
 r
5.1.1.10 L-Leu
-
 Pyrococcus horikoshii OT-3 D-Leu
-
 r
5.1.1.10 L-leucine
-
 Pyrococcus horikoshii D-leucine
-
 r
5.1.1.10 L-Met
-
 Pyrococcus horikoshii D-Met
-
 r
5.1.1.10 L-Met
-
 Pyrococcus horikoshii OT-3 D-Met
-
 r
5.1.1.10 L-Methionine
-
 Pyrococcus horikoshii D-Methionine
-
 r
5.1.1.10 L-Phe
-
 Pyrococcus horikoshii D-Phe
-
 r
5.1.1.10 L-phenylalanine
-
 Pyrococcus horikoshii D-phenylalanine
-
 r
5.1.1.10 L-serine
-
 Pyrococcus horikoshii D-serine
-
 r
5.1.1.10 L-threonine
-
 Pyrococcus horikoshii D-threonine
-
 r
5.1.1.10 L-Trp
-
 Pyrococcus horikoshii D-Trp
-
 r
5.1.1.10 L-tryptophan
-
 Pyrococcus horikoshii D-tryptophan
-
 r
5.1.1.10 L-Tyr
-
 Pyrococcus horikoshii D-Tyr
-
 r
5.1.1.10 L-tyrosine
-
 Pyrococcus horikoshii D-tyrosine
-
 r
5.1.1.10 L-Val
-
 Pyrococcus horikoshii D-Val
-
 r
5.1.1.10 L-valine
-
 Pyrococcus horikoshii D-valine
-
 r
5.1.1.10 additional information the enzyme predominantly shows activity toward hydrophobic and aromatic amino acids. No activity toward Arg, His, Gln, and Asn Pyrococcus horikoshii ?
-
 ?
5.1.1.10 additional information the enzyme BAR has broad substrate specificity, it is active toward Met, Leu, Phe, Ile, Val, Ala, Trp, Tyr, Thr, and Ser, but no activity toward Pro, Asp, Glu, Arg, His, Gln, Cys, Lys, and Asn. In particular, the high reaction rate with Trp and Tyr, in addition to Leu, Met and Phe as substrates is a noteworthy feature of this enzyme. Histochemic analysis of D- and L-amino acid products. The Vmax values obtained with Ala, Val, Ile, Leu, and Met in D-amino acid forming reactions are lower than in L-amino acid forming reactions. By contrast, the Vmax values for Phe, Tyr, and Trp in D-amino acid forming reactions are higher than in L-amino acid forming reaction. The D-forms of Arg, His, Asn, and Gln are not quantitatively detected Pyrococcus horikoshii ?
-
 ?
5.1.1.10 additional information the enzyme predominantly shows activity toward hydrophobic and aromatic amino acids. No activity toward Arg, His, Gln, and Asn Pyrococcus horikoshii OT-3 ?
-
 ?
5.1.1.10 additional information the enzyme BAR has broad substrate specificity, it is active toward Met, Leu, Phe, Ile, Val, Ala, Trp, Tyr, Thr, and Ser, but no activity toward Pro, Asp, Glu, Arg, His, Gln, Cys, Lys, and Asn. In particular, the high reaction rate with Trp and Tyr, in addition to Leu, Met and Phe as substrates is a noteworthy feature of this enzyme. Histochemic analysis of D- and L-amino acid products. The Vmax values obtained with Ala, Val, Ile, Leu, and Met in D-amino acid forming reactions are lower than in L-amino acid forming reactions. By contrast, the Vmax values for Phe, Tyr, and Trp in D-amino acid forming reactions are higher than in L-amino acid forming reaction. The D-forms of Arg, His, Asn, and Gln are not quantitatively detected Pyrococcus horikoshii OT-3 ?
-
 ?

Subunits

EC Number Subunits Comment Organism
5.1.1.10 dimer 2 * 52100, SDS-PAGE Pyrococcus horikoshii
5.1.1.10 homodimer 2 * 55800, recombinant enzyme, SDS-PAGE, 2 * 52100, about, sequence calculation Pyrococcus horikoshii

Synonyms

EC Number Synonyms Comment Organism
5.1.1.10 AAR
-
 Pyrococcus horikoshii
5.1.1.10 amino acid racemase
-
 Pyrococcus horikoshii
5.1.1.10 BAR
-
 Pyrococcus horikoshii
5.1.1.10 broad substrate specificity amino acid racemase
-
 Pyrococcus horikoshii
5.1.1.10 PH0138
-
 Pyrococcus horikoshii

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
5.1.1.10 80
-
 assay at Pyrococcus horikoshii
5.1.1.10 95
-
-
 Pyrococcus horikoshii
5.1.1.10 95
-
 or above Pyrococcus horikoshii

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
5.1.1.10 50 80 the relative activities at 50°C and 80°C are 12% and 70%, respectively, as compared with that at 95°C Pyrococcus horikoshii
5.1.1.10 50 95 activity range, the relative activities at 50°C and 80°C are 12% and 70%, respectively, as compared with that at 95°C Pyrococcus horikoshii

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
5.1.1.10 80
-
 enzyme retains its full activity after incubation at 80°C for at least 2 h in buffer pH 7-10 Pyrococcus horikoshii
5.1.1.10 80
-
 purified enzyme protein at 80°C for 2 h under various pH conditions, BAR shows no loss of activity at pHs ranging from pH 7.0 to pH 10.0. At pH 7.0, the enzyme retains its full activity, even after incubation at 80°C for 24 h Pyrococcus horikoshii

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
5.1.1.10 6.5 7.5 at a temperature of 60°C, the highest activity is detected at around pH 6.5-7.5 Pyrococcus horikoshii
5.1.1.10 6.5 7.5 at 60°C, the highest activity is detected at around pH 6.5-7.5 Pyrococcus horikoshii
5.1.1.10 7
-
 assay at Pyrococcus horikoshii

pH Range

EC Number pH Minimum pH Maximum Comment Organism
5.1.1.10 6 10 over 80% of maximal activity within this range, about 40% at pH 4.0, and about 50% at pH 11.0 Pyrococcus horikoshii

Cofactor

EC Number Cofactor Comment Organism Structure
5.1.1.10 pyridoxal 5'-phosphate dependent on Pyrococcus horikoshii

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
5.1.1.10 0.159
-
 L-Ala pH 7.0, 80°C Pyrococcus horikoshii
5.1.1.10 0.159
-
 L-alanine pH 7.0, 80°C, recombinant enzyme Pyrococcus horikoshii
5.1.1.10 0.75
-
 D-alanine pH 7.0, 80°C, recombinant enzyme Pyrococcus horikoshii
5.1.1.10 0.95
-
 D-Ala pH 7.0, 80°C Pyrococcus horikoshii
5.1.1.10 1.31
-
 D-Trp pH 7.0, 80°C Pyrococcus horikoshii
5.1.1.10 1.31
-
 D-tryptophan pH 7.0, 80°C, recombinant enzyme Pyrococcus horikoshii
5.1.1.10 1.97
-
 L-Val pH 7.0, 80°C Pyrococcus horikoshii
5.1.1.10 1.97
-
 L-valine pH 7.0, 80°C, recombinant enzyme Pyrococcus horikoshii
5.1.1.10 2.39
-
 L-Trp pH 7.0, 80°C Pyrococcus horikoshii
5.1.1.10 2.39
-
 L-tryptophan pH 7.0, 80°C, recombinant enzyme Pyrococcus horikoshii
5.1.1.10 2.67
-
 D-Val pH 7.0, 80°C Pyrococcus horikoshii
5.1.1.10 2.67
-
 D-valine pH 7.0, 80°C, recombinant enzyme Pyrococcus horikoshii
5.1.1.10 4.12
-
 D-Ile pH 7.0, 80°C Pyrococcus horikoshii
5.1.1.10 4.12
-
 D-isoleucine pH 7.0, 80°C, recombinant enzyme Pyrococcus horikoshii
5.1.1.10 5.5
-
 L-Ile pH 7.0, 80°C Pyrococcus horikoshii
5.1.1.10 5.5
-
 L-isoleucine pH 7.0, 80°C, recombinant enzyme Pyrococcus horikoshii
5.1.1.10 5.69
-
 D-Tyr pH 7.0, 80°C Pyrococcus horikoshii
5.1.1.10 5.69
-
 D-tyrosine pH 7.0, 80°C, recombinant enzyme Pyrococcus horikoshii
5.1.1.10 8.26
-
 L-Met pH 7.0, 80°C Pyrococcus horikoshii
5.1.1.10 8.26
-
 L-methionine pH 7.0, 80°C, recombinant enzyme Pyrococcus horikoshii
5.1.1.10 11
-
 L-Phe pH 7.0, 80°C Pyrococcus horikoshii
5.1.1.10 11
-
 L-phenylalanine pH 7.0, 80°C, recombinant enzyme Pyrococcus horikoshii
5.1.1.10 11.4
-
 L-Tyr pH 7.0, 80°C Pyrococcus horikoshii
5.1.1.10 11.4
-
 L-tyrosine pH 7.0, 80°C, recombinant enzyme Pyrococcus horikoshii
5.1.1.10 11.9
-
 L-Leu pH 7.0, 80°C Pyrococcus horikoshii
5.1.1.10 11.9
-
 L-leucine pH 7.0, 80°C, recombinant enzyme Pyrococcus horikoshii
5.1.1.10 12.7
-
 D-Met pH 7.0, 80°C Pyrococcus horikoshii
5.1.1.10 12.7
-
 D-methionine pH 7.0, 80°C, recombinant enzyme Pyrococcus horikoshii
5.1.1.10 18.4
-
 D-Leu pH 7.0, 80°C Pyrococcus horikoshii
5.1.1.10 18.4
-
 D-leucine pH 7.0, 80°C, recombinant enzyme Pyrococcus horikoshii
5.1.1.10 19.9
-
 D-Phe pH 7.0, 80°C Pyrococcus horikoshii
5.1.1.10 19.9
-
 D-phenylalanine pH 7.0, 80°C, recombinant enzyme Pyrococcus horikoshii