Information on EC 5.4.3.10 - phenylalanine aminomutase (L-beta-phenylalanine forming)

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: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
5.4.3.10
-
RECOMMENDED NAME
GeneOntology No.
phenylalanine aminomutase (L-beta-phenylalanine forming)
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-phenylalanine = D-beta-phenylalanine
show the reaction diagram
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
3-amino-3-phenylpropanoyl-CoA biosynthesis
-
-
phenylalanine metabolism
-
-
SYSTEMATIC NAME
IUBMB Comments
L-phenylalanine 2,3-aminomutase [(R)-3-amino-3-phenylpropanoate forming]
The enzyme contains the cofactor 3,5-dihydro-5-methylidene-4H-imidazol-4-one (MIO). This unique cofactor is formed autocatalytically by cyclization and dehydration of the three amino-acid residues alanine, serine and glycine. cf. EC 5.4.3.11, phenylalanine aminomutase (D-beta-phenylalanine forming).
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3'-methyl-alpha-phenylalanine
3'-methyl-beta-phenylalanine
show the reaction diagram
-
plus 3'-methylcinnamate, product of ammonia lyase reaction. Distribution of 3'-methyl-beta-phenylalanine and 3'-methylcinnamate is at about 1:1
-
?
4'-methyl-alpha-phenylalanine
4'-methyl-beta-phenylalanine
show the reaction diagram
-
plus 4'-methylcinnamate, product of ammonia lyase reaction
-
?
L-phenylalanine
L-beta-phenylalanine
show the reaction diagram
-
-
-
?
styryl-alpha-alanine
5-phenyl-(2E,4E)-pentadienoate
show the reaction diagram
-
-
-
?
additional information
?
-
(E)-cinnamate is both a substrate and an intermediate of the reaction. To account for the distinct (3alpha)-beta-amino acid stereochemistry catalyzed by the enzyme, the cinnamate skeleton must rotate the C1-Calpha and Cipso-Cbeta bonds 180° in the active site prior to exchange and rebinding of theNH2/H pair to the cinnamate
-
-
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4-methylidene-1H-imidazol-5(4H)-one
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.083 - 0.397
3'-methyl-alpha-phenylalanine
0.073 - 0.091
4'-methyl-alpha-phenylalanine
0.057 - 0.136
L-phenylalanine
0.12 - 0.25
styryl-alpha-alanine
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.022 - 0.028
3'-methyl-alpha-phenylalanine
0.02 - 0.03
4'-methyl-alpha-phenylalanine
0.003 - 0.053
L-phenylalanine
0.0002 - 0.003
styryl-alpha-alanine
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.055 - 0.34
3'-methyl-alpha-phenylalanine
19754
0.27 - 0.33
4'-methyl-alpha-phenylalanine
19755
0.022 - 0.93
L-phenylalanine
104
0.025
styryl-alpha-alanine
Taxus canadensis
Q6GZ04
mutant L104A, pH 8.5, 31°C
19756
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
to 2.38 A resolution, space group C2. A (E)-cinnamate molecule is bound in the active site, lying above the 4-methylidene-1H-imidazol-5(4H)-one cofactor and under a loop region that includes residues 80-97, which define the top of the active site. The (E)-cinnamate molecule lies about 3.4 A above the methylidene carbon of the 4-methylidene-1H-imidazol-5(4H)-one moiety. The carboxylate of the cinnamate makes a salt bridge interaction with a strongly conserved residue R325, which serves to position the product in the active site. The plane of the aromatic ring of the cinnamate is displaced about 20° from the perpendicular relative to the pi-bond plane of the propenoate carboncarbon double bond. The aromatic ring is bound relatively loosely in the active site, making only one direct hydrophobic interaction with residue L104
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
L104A
1.5-fold increase in kcat and a decrease in KM values for 3'-methyl-alpha-phenylalanine and styryl-alpha-alanine substrates