5.1.1.21: isoleucine 2-epimerase
This is an abbreviated version!
For detailed information about isoleucine 2-epimerase, go to the full flat file.
Word Map on EC 5.1.1.21
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5.1.1.21
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buchneri
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racemization
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lactobacillus
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epimerization
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5'-phosphate
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pyridoxal
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nonpolar
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d-leucine
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diaminopimelate
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two-base
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l-isoleucine
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d-valine
- 5.1.1.21
- buchneri
-
racemization
- lactobacillus
-
epimerization
- 5'-phosphate
- pyridoxal
-
nonpolar
- d-leucine
- diaminopimelate
-
two-base
- l-isoleucine
- d-valine
Reaction
Synonyms
amino acid racemase, BCAA racemase, branched-chain amino-acid racemase, D-amino acid racemase, DAAR1, ILEP, isoleucine 2-epimerase, phenazine biosynthesis PhzC/PhzF family protein, PLP-dependent fold-type I isoleucine 2-epimerase, PLP-independent racemase
ECTree
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Substrates Products
Substrates Products on EC 5.1.1.21 - isoleucine 2-epimerase
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REACTION DIAGRAM
(R)-2-aminobutyric acid
(S)-2-aminobutyric acid
activity is 42% compared to D-allo-isoleucine
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-
r
(S)-2-aminobutyric acid
(R)-2-aminobutyric acid
activity is 32% compared to L-isoleucine
-
-
r
D-leucine
L-leucine
activity is 30% compared to D-allo-isoleucine
-
-
?
D-methionine
L-methionine
activity is 20% compared to D-allo-isoleucine
-
-
?
D-norleucine
L-norleucine
activity is 59% compared to D-allo-isoleucine
-
-
r
D-phenylalanine
L-phenylalanine
activity is 25% compared to D-allo-isoleucine
-
-
?
D-valine
L-Val
activity is 52% compared to D-allo-isoleucine
-
-
r
L-phenylalanine
D-phenylalanine
activity is 24% compared to L-isoleucine
-
-
?
L-valine
D-Val
activity is 48% compared to L-isoleucine
-
-
r
L-norvaline
activity is 83% compared to D-allo-isoleucine
-
-
r
D-norvaline
L-norvaline
activity is 83% compared to D-allo-isoleucine
-
-
r
L-leucine
D-leucine
activity is 30% compared to L-isoleucine
-
-
?
D-Methionine
activity is 19% compared to L-isoleucine
-
-
?
L-Methionine
D-Methionine
activity is 19% compared to L-isoleucine
-
-
?
D-Norleucine
activity is 50% compared to L-isoleucine
-
-
r
L-Norleucine
D-Norleucine
activity is 50% compared to L-isoleucine
-
-
r
D-Norvaline
activity is 56% compared to L-isoleucine
-
-
r
L-Norvaline
D-Norvaline
activity is 56% compared to L-isoleucine
-
-
r
?
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the enzyme does not require pyridoxal 5'-phosphate for its activity. Compared with Ile, DAAR1 shows 1 and 5% relative activity toward Leu and Val, respectively. DAAR1 shows no activity toward N-acetyl-L-Ile, a commercially available surrogate for N-malonyl-L-Ile, suggesting that DAAR1 does not use a N-derivatized substrate
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-
?
additional information
?
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-
the enzyme does not require pyridoxal 5'-phosphate for its activity. Compared with Ile, DAAR1 shows 1 and 5% relative activity toward Leu and Val, respectively. DAAR1 shows no activity toward N-acetyl-L-Ile, a commercially available surrogate for N-malonyl-L-Ile, suggesting that DAAR1 does not use a N-derivatized substrate
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-
?
additional information
?
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the enzyme specifically catalyzes racemization of nonpolar amino acids at the C-2 position. No activity toward the L- and D-forms of Asp, Glu, Lys, Arg, His, Orn, Thr, Asn, Gln, Trp, and tert-Leu
-
-
?
additional information
?
-
-
the enzyme specifically catalyzes racemization of nonpolar amino acids at the C-2 position. No activity toward the L- and D-forms of Asp, Glu, Lys, Arg, His, Orn, Thr, Asn, Gln, Trp, and tert-Leu
-
-
?
additional information
?
-
the enzyme catalyzes the pyridoxal 5'-phosphate (PLP)-dependent racemization and epimerization of a broad spectrum of nonpolar amino acids from L- to D-form and vice versa, in particular isoleucine
-
-
?
additional information
?
-
-
the enzyme catalyzes the pyridoxal 5'-phosphate (PLP)-dependent racemization and epimerization of a broad spectrum of nonpolar amino acids from L- to D-form and vice versa, in particular isoleucine
-
-
?
additional information
?
-
the enzyme specifically catalyzes racemization of nonpolar amino acids at the C-2 position. No activity toward the L- and D-forms of Asp, Glu, Lys, Arg, His, Orn, Thr, Asn, Gln, Trp, and tert-Leu
-
-
?
additional information
?
-
the enzyme catalyzes the pyridoxal 5'-phosphate (PLP)-dependent racemization and epimerization of a broad spectrum of nonpolar amino acids from L- to D-form and vice versa, in particular isoleucine
-
-
?