5.1.1.11: phenylalanine racemase (ATP-hydrolysing)
This is an abbreviated version!
For detailed information about phenylalanine racemase (ATP-hydrolysing), go to the full flat file.
Word Map on EC 5.1.1.11
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5.1.1.11
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brevis
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racemization
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nonribosomal
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adenylate
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thioester
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three-domain
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synthetases
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decapeptide
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aminoacyl
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epimerization
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nagano
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triphosphate-dependent
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single-turnover
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non-producing
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diester
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d-phe
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equilibrate
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thiolation
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4'-phosphopantetheine
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phenylalanyl
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synthesis
- 5.1.1.11
- brevis
-
racemization
-
nonribosomal
- adenylate
- thioester
-
three-domain
- synthetases
-
decapeptide
-
aminoacyl
-
epimerization
-
nagano
-
triphosphate-dependent
-
single-turnover
-
non-producing
-
diester
- d-phe
-
equilibrate
-
thiolation
- 4'-phosphopantetheine
-
phenylalanyl
- synthesis
Reaction
Synonyms
Gramicidin S synthetase I, GrsA, GS I, PheATE, Phenylalanine racemase, Phenylalanine racemase (adenosine triphosphate-hydrolyzing), Phenylalanine racemase (ATP-hydrolyzing), Racemase, phenylalanine (adenosine triphosphate-hydrolyzing)
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Reaction
Reaction on EC 5.1.1.11 - phenylalanine racemase (ATP-hydrolysing)
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the enzyme activates both L-Phe and D-Phe to form L-phenylalanyl adenylate and D-phenylalanyl adenylate bound to the enzyme, respectively, and then transfers the L-Phe and D-Phe moiety to the thiol group of the enzyme followed by conversion of its configuration, the D-isomer being the more favorable configuration
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ATP + L-phenylalanine + H2O = AMP + diphosphate + D-phenylalanine
racemizes Phe in the thioester-bound stage
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ATP + L-phenylalanine + H2O = AMP + diphosphate + D-phenylalanine
phenylalanine racemase catalyzes the exchange between a proton in the medium and alpha-hydrogen of Phe. Probably a sulfhydryl group, on the enzyme functions as proton donor and acceptor during the reaction
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ATP + L-phenylalanine + H2O = AMP + diphosphate + D-phenylalanine
the amino group of Phe is essential for its binding to the aminoacyl adenylate reaction center. The carbonyl group is not at all or only weakly bound. The benzene ring of Phe which determines substrate recognition also seems to be of minor importance for substrate binding
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