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Literature summary for 2.6.1.B21 extracted from

  • Bezsudnova, E.Y.; Dibrova, D.V.; Nikolaeva, A.Y.; Rakitina, T.V.; Popov, V.O.
    Identification of branched-chain amino acid aminotransferases active towards (R)-(+)-1-phenylethylamine among PLP fold type IV transaminases (2018), J. Biotechnol., 271, 26-28 .
    View publication on PubMed
Search for more literature for 2.6.1.B21

Cloned(Commentary)

Cloned (Comment) Organism
gene ilvE, recombinant expression of codon-optimized gene encoding the His6-tagged enzyme with TEV proteae cleavage site in Escherichia coli strain BL21(DE3)pLys Haliangium ochraceum

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
11.8
-
 (R)-1-phenylethylamine pH 9.0, 40°C, recombinant enzyme, with 3-methyl-2-oxovalerate Haliangium ochraceum

Organism

Organism UniProt Comment Textmining
Haliangium ochraceum D0LR31
-
-
Haliangium ochraceum DSM 14365 D0LR31
-
-
Haliangium ochraceum JCM 11303 D0LR31
-
-
Haliangium ochraceum SMP-2 D0LR31
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3)pLys by nickel affinity chromatography, tag cleavage by TEV protease, and gel filtration, to homogeneity Haliangium ochraceum

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.007
-
 purified recombinant enzyme, pH 8.0, 40°C, substrates (R)-1-phenylethylamine and 3-methyl-3-oxovalerate Haliangium ochraceum
0.1
-
 purified recombinant enzyme, pH 9.0, 40°C, substrates (R)-1-phenylethylamine and 3-methyl-3-oxovalerate Haliangium ochraceum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(R)-1-phenylethylamine + 3-methyl-2-oxovalerate the enzyme is active towards (R)-PEA and not active towards (S)-PEA Haliangium ochraceum acetophenone + L-isoleucine
-
 r
(R)-1-phenylethylamine + 3-methyl-2-oxovalerate the enzyme is active towards (R)-PEA and not active towards (S)-PEA Haliangium ochraceum JCM 11303 acetophenone + L-isoleucine
-
 r
(R)-1-phenylethylamine + 3-methyl-2-oxovalerate the enzyme is active towards (R)-PEA and not active towards (S)-PEA Haliangium ochraceum DSM 14365 acetophenone + L-isoleucine
-
 r
(R)-1-phenylethylamine + 3-methyl-2-oxovalerate the enzyme is active towards (R)-PEA and not active towards (S)-PEA Haliangium ochraceum SMP-2 acetophenone + L-isoleucine
-
 r
additional information no activity with 2-oxoglutarate and with beta-Ala and D-Ala. The deamination of L-Leu and L-Ile by the transaminase from Haliangium ochraceum is observed only in half-reactions. Reaction mechanisms Haliangium ochraceum ?
-
-
additional information no activity with 2-oxoglutarate and with beta-Ala and D-Ala. The deamination of L-Leu and L-Ile by the transaminase from Haliangium ochraceum is observed only in half-reactions. Reaction mechanisms Haliangium ochraceum JCM 11303 ?
-
-
additional information no activity with 2-oxoglutarate and with beta-Ala and D-Ala. The deamination of L-Leu and L-Ile by the transaminase from Haliangium ochraceum is observed only in half-reactions. Reaction mechanisms Haliangium ochraceum DSM 14365 ?
-
-
additional information no activity with 2-oxoglutarate and with beta-Ala and D-Ala. The deamination of L-Leu and L-Ile by the transaminase from Haliangium ochraceum is observed only in half-reactions. Reaction mechanisms Haliangium ochraceum SMP-2 ?
-
-

Synonyms

Synonyms Comment Organism
(R)-selective (R)-amine:pyruvate transaminase
-
 Haliangium ochraceum
Hoch3033
-
 Haliangium ochraceum
More cf. EC 2.6.1.42 Haliangium ochraceum

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
40
-
-
 Haliangium ochraceum

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.19
-
 (R)-1-phenylethylamine pH 9.0, 40°C, recombinant enzyme, with 3-methyl-2-oxovalerate Haliangium ochraceum

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
9
-
 (R)-transamination with (R)-phenylethylamine Haliangium ochraceum

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate PLP Haliangium ochraceum

General Information

General Information Comment Organism
evolution the enzyme belongs to the PLP fold type IV transaminases Haliangium ochraceum

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.016
-
 (R)-1-phenylethylamine pH 9.0, 40°C, recombinant enzyme, with 3-methyl-2-oxovalerate Haliangium ochraceum