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ATP + L-phenylalanine + H2O = AMP + diphosphate + D-phenylalanine
ATP + L-phenylalanine + H2O = AMP + diphosphate + D-phenylalanine
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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ATP + L-phenylalanine + H2O = AMP + diphosphate + D-phenylalanine
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ATP + 4-fluoro-DL-Phe + H2O
?
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-
-
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?
ATP + L-Phe + H2O
AMP + diphosphate + D-Phe
ATP + L-phenylalanine + H2O
?
ATP + L-phenylalanine + H2O
AMP + diphosphate + D-phenylalanine
ATP + L-Tyr + H2O
AMP + diphosphate + D-Tyr
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-
-
-
?
ATP + p-fluoro-L-Phe + H2O
AMP + diphosphate + p-fluoro-D-Phe
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-
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?
additional information
?
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the enzyme catalyzes Phe racemization and activation. Catalyzes ATP-AMP exchange reaction, L-Phe dependent ATP-AMP exchange reaction
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ATP + L-Phe + H2O
AMP + diphosphate + D-Phe
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?
ATP + L-Phe + H2O
AMP + diphosphate + D-Phe
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?
ATP + L-Phe + H2O
AMP + diphosphate + D-Phe
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-
?
ATP + L-Phe + H2O
AMP + diphosphate + D-Phe
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-
?
ATP + L-Phe + H2O
AMP + diphosphate + D-Phe
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?
ATP + L-Phe + H2O
AMP + diphosphate + D-Phe
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-
?
ATP + L-Phe + H2O
AMP + diphosphate + D-Phe
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?
ATP + L-Phe + H2O
AMP + diphosphate + D-Phe
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?
ATP + L-Phe + H2O
AMP + diphosphate + D-Phe
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?
ATP + L-Phe + H2O
AMP + diphosphate + D-Phe
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?
ATP + L-Phe + H2O
AMP + diphosphate + D-Phe
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?
ATP + L-Phe + H2O
AMP + diphosphate + D-Phe
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?
ATP + L-Phe + H2O
AMP + diphosphate + D-Phe
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?
ATP + L-Phe + H2O
AMP + diphosphate + D-Phe
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?
ATP + L-Phe + H2O
AMP + diphosphate + D-Phe
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?
ATP + L-Phe + H2O
AMP + diphosphate + D-Phe
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?
ATP + L-Phe + H2O
AMP + diphosphate + D-Phe
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?
ATP + L-Phe + H2O
AMP + diphosphate + D-Phe
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?
ATP + L-Phe + H2O
AMP + diphosphate + D-Phe
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?
ATP + L-Phe + H2O
AMP + diphosphate + D-Phe
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equilibrium ratio of L-Phe to D-Phe is 3:7
-
?
ATP + L-phenylalanine + H2O
?
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phenylalanine racemase, i.e. gramicidin-S synthetase 1, activates and transfers D-Phe to the heavy enzyme, gramicidin S-synthetase 2, which activates the other constituent amino acids on the thioester template
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?
ATP + L-phenylalanine + H2O
?
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phenylalanine racemase, the light component of gramicidin S synthetase, racemizes Phe and activates it to the aminoacyl adenylate and in a second step to the thioester
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?
ATP + L-phenylalanine + H2O
AMP + diphosphate + D-phenylalanine
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there are three activated intermediates: L-phenylalanyl-adenosine-5'-monophosphate diester, L-Phe-S-4'-phosphopantetheine and D-Phe-S-4'-phosphopantetheine-acyl enzyme
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?
ATP + L-phenylalanine + H2O
AMP + diphosphate + D-phenylalanine
-
the three-domain initiation module PheATE of gramicidin S synthetase catalyzes the activation, thiolation and epimerization of L-phenylalanine, the first amino acid incorporated into the decapeptide antibiotic gramicidin S
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?
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Adams, E.
Amino acid racemases and epimerases
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
6
479-507
1972
Brevibacillus brevis
-
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Yamada, M.; Kurahashi, K.
Adenosine triphosphate and pyrophosphate dependent phenylalanine racemase of Bacillus brevis Nagano
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Further purification and properties of adenosine triphosphate-dependent phenylalanine racemase of Bacillus brevis NAGANO
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Vater, J.; Kleinkauf, H.
Gramicidin S synthetase. A further characterization of phenylalanine racemase, the light enzyme of gramicidin S-synthetase
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Mutant genes of gramicidin S synthetase 1 defective in phenylalanine racemization have the same sequence as the wild gene
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Nguyen Huu, M.C.; von Dungen, A.; Kleinkauf, H.
Irreversible inhibition of the light enzyme of gramicidin S synthetase by halogenomethylketones of phenylalanine
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67
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Brevibacillus brevis
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91
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Vater, J.; Mallow, N.; Gerhardt, S.; Kleinkauf, H.
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1982
Brevibacillus brevis
-
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Vater, J.; Mallow, N.; Gerhardt, S.; Gadow, A.; Kleinkauf, H.
Gramicidin S synthetase. Temperature dependence and thermodynamic parameters of substrate amino acid activation reactions
Biochemistry
24
2022-2027
1985
Brevibacillus brevis
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Schroeter-Kermani, C.; von Dhren, H.; Kleinkauf, H.
Active thiol-directed binding and adsorption of gramicidin S-synthetase I to disulfide-containing matrices
Biochim. Biophys. Acta
883
345-352
1986
Brevibacillus brevis
-
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Schlunsen, J.; Manecke, G.
Spezifische Adsorbentien fur das Peptidantibiotika synthetisierende Enzymsystem Gramicidin S Synthetase, 1. Darstellung niedermolekularer Spacer-Ligand-Verbindungen
Makromol. Chem.
188
3005-3016
1987
Brevibacillus brevis
-
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Kambe, M.; Imae, Y.; Kurahashi, K.
Biochemical studies on gramicidin S non-producing mutants of Bacillus brevis ATCC 9999
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75
481-493
1974
Brevibacillus brevis
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Kanda, M.; Hori, K.; Kurotsu, T.; Miura, S.; Yamada, Y.; Saito, Y.
Sulfhydryl groups related to the catalytic activity of gramicidin S synthetase 1 of Bacillus brevis
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90
765-771
1981
Brevibacillus brevis
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Saito, Y.
Some characteristics of gramicidin S-synthetase obtained from mutants of Bacillus brevis which could not form D-phenylalanyl-L-prolyl diketo-piperazine
Pept. Antibiot.
1982
195-207
1982
Brevibacillus brevis
-
brenda
Matteo, C.C.; Cooney, C.L.; Demain, A.L.
Production of gramicidin S synthetases by Bacillus brevis in continuous culture
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96
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1976
Brevibacillus brevis
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Racemization of phenylalanine by adenosine triphosphate-dependent phenylalanine racemase of Bacillus brevis Nagano
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69
973-976
1971
Brevibacillus brevis
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Kanda, M.; Hori, K.; Kurotsu, T.; Miura, S.; Saito, Y.
Reaction mechanism of gramicidin S synthetase 1, phenylalanine racemase, of Bacillus brevis
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105
653-659
1989
Brevibacillus brevis
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Stein, T.; Kluge, B.; Vater, J.; Franke, P.; Otto, A.; Wittmann-Liebold, B.
Gramicidin S synthetase 1 (phenylalanine racemase), a prototype of amino acid racemase containing the cofactor 4'-phosphopantetheine
Biochemistry
34
4633-4642
1995
Brevibacillus brevis
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Vater, J.; Schlumbohm, W.; Salnikow, J.; Irrgang, K.D.; Miklus, M.; Choli, T.; Kleinkauf, H.
Proteinchemical and kinetic features of gramicidin S synthetase
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370
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1989
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Stachelhaus, T.; Walsh, C.T.
Mutational analysis of the epimerization domain in the initiation module PheATE of gramicidin S synthetase
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Brevibacillus brevis
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Luo, L.; Walsh, C.T.
Kinetic analysis of three activated phenylalanyl intermediates generated by the initiation module PheATE of gramicidin S synthetase
Biochemistry
40
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Biochemical evidence for conformational changes in the cross-talk between adenylation and peptidyl-carrier protein domains of nonribosomal peptide synthetases
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