Information on EC 5.1.1.11 - phenylalanine racemase (ATP-hydrolysing)

Word Map on EC 5.1.1.11
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


The expected taxonomic range for this enzyme is: Brevibacillus brevis

EC NUMBER
COMMENTARY hide
5.1.1.11
-
RECOMMENDED NAME
GeneOntology No.
phenylalanine racemase (ATP-hydrolysing)
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + L-phenylalanine + H2O = AMP + diphosphate + D-phenylalanine
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
racemization
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Phenylalanine metabolism
-
-
phenylalanine metabolism
-
-
SYSTEMATIC NAME
IUBMB Comments
phenylalanine racemase (ATP-hydrolysing)
-
CAS REGISTRY NUMBER
COMMENTARY hide
37290-95-2
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + L-Phe + H2O
AMP + diphosphate + D-Phe
show the reaction diagram
ATP + L-phenylalanine + H2O
?
show the reaction diagram
ATP + L-phenylalanine + H2O
AMP + diphosphate + D-phenylalanine
show the reaction diagram
ATP + L-Tyr + H2O
AMP + diphosphate + D-Tyr
show the reaction diagram
-
-
-
-
-
ATP + p-fluoro-L-Phe + H2O
AMP + diphosphate + p-fluoro-D-Phe
show the reaction diagram
-
-
-
-
-
additional information
?
-
-
the enzyme catalyzes Phe racemization and activation. Catalyzes ATP-AMP exchange reaction, L-Phe dependent ATP-AMP exchange reaction
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + L-phenylalanine + H2O
?
show the reaction diagram
ATP + L-phenylalanine + H2O
AMP + diphosphate + D-phenylalanine
show the reaction diagram
-
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
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4'-phosphopantetheine
-
a 4'-phosphopantetheine carrier is found to be attached to the active site Ser of the consensus motif LGGDSI forming the thiolation site of Phe
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
-
Mn2+ or Mg2+ required, up to 0.5 mM. Inhibitory at higher concentrations
Mn2+
-
Mn2+ or Mg2+ required, up to 0.5 mM
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-Phenylethylamine
-
-
5,5'-dithiobis(2-nitrobenzoate)
-
presence of ATP, MgCl2, and dithiothreitol prevent rapid sulfhydryl modification. With the enzyme of a gramicidin S non-producing and phenylalanine racemization-lacking mutant the substrate protection against rapid sulfhydryl modification is not detected
cystamine
-
Mg2+ alone or in combination with the substrates ATP and Phe causes significant protection. Cystamine-inactivated enzyme can be reactivated by treatment with dithioerythritol or other sulfhydryl compounds. 0.5 M cystamine causes 90%, 40% and 30% loss in activity if preincubated at 37C, 20C, or 0C for 20 min
cysteamine
-
-
DL-cystine
-
-
Hydrocinnamic acid
-
-
hydroxylamine
-
-
Isoniazid
-
-
L-1-Bromo-3-amino-4-phenyl-butan-2-one
-
irreversible
L-1-Chloro-3-amino-4-phenyl-butan-2-one
-
irreversible
N,N'-Diacetylcystamine
-
-
Phenylglyoxal
-
inhibition of Phe activation. Both ATP and Phe prevent the inactivation. ATP is competitive with phenylglyoxal, whereas Phe is not. A single arginine residue of GS 1 is essential for Phe activation in binding the phosphate moiety of ATP
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
-
stimulates 2-2.5fold at 0.05 M
diphosphate
-
absolute requirement. Optimal concentration: 0.2-2 mM
dithiothreitol
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.15
ATP
-
-
0.13
D-Phe
-
-
0.0062 - 0.06
L-Phe
2.1
L-Tyr
-
-
1.4
p-fluoro-DL-Phe
-
-
additional information
additional information
-
temperature dependence of Km-values
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.25 - 0.38
L-Phe
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.8
-
formation of L-isomer from D-Phe
8.2 - 8.5
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.2 - 8.6
-
7.2: about 25% of maximal activity, 8.6: about 85% of maximal activity
additional information
-
the velocity of the D-Phe formation from the L-isomer is markedly affected by the concentration of DTT, whereas that of L-Phe formation from the D-isomer is less affected
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
73900
holo-A-PCP-form (GrsA plus peptidyl carrier protein domain), gel-filtration
74200
apo-A-PCP-form (GrsA plus peptidyl carrier protein domain), gel-filtration
95000
-
x * 95000, SDS-PAGE
100000
118000
-
1 * 118000, SDS-PAGE
132000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
-
1 * 118000, SDS-PAGE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
specific adsorbents, spacer/ligand compounds
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli as a C-terminal His tag fusion
-
mutant genes of gramicidin-S synthetase 1 defective in Phe racemization have the same sequence as the wild type gene. These mutant strains also produce defective gramicidin S synthetase 2, lacking 4'-phosphopantetheine, a prosthetic group of this enzyme. The participation of this group in phenylalanine racemization is suggested
-
overexpressed as a C-terminal His6-tag protein in Escherichia coli BL21 (DE3)
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C331A
minor changes in activity or specificity
C331L
activity of GrsA is decreased to 26%
C376S
no changes in activity
C473A
no changes in activity
C60F
no changes in activity
C60F/C331A/C376S/C473A
named A-PCP(delta-4Cys), Km for L-Phe is increased by 2fold, while the kcat is reduced by 1.5fold
D767S
-
mutant enzyme is impaired in approach to D-Phe/L-Phe-S-4'phosphopantetheine equilibrium only for D-Phe to L-Phe direction
E892A
-
mutant enzyme is dramatically impaired in approach to D-Phe/L-Phe-S-4'phosphopantetheine equilibrium from either D-Phe or L-Phe; only slightly active with L-Phe, unimpaired reaction with D-Phe
H753A
-
only slightly active with L-Phe, unimpaired reaction with D-Phe
R896A
-
mutant enzyme is dramatically impaired in approach to D-Phe/L-Phe-S-4'phosphopantetheine equilibrium from either D-Phe or L-Phe
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
-
production of phenylalanine racemase in continuous culture
Show AA Sequence (552 entries)
Please use the Sequence Search for a specific query.