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Information on EC 5.4.3.10 - phenylalanine aminomutase (L-beta-phenylalanine forming) and Organism(s) Taxus canadensis and UniProt Accession Q6GZ04

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EC Tree
IUBMB Comments
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).
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This record set is specific for:
Taxus canadensis
UNIPROT: Q6GZ04
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Word Map
The taxonomic range for the selected organisms is: Taxus canadensis
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
tcpam, phenylalanine aminomutase, phenylalanine-2,3-aminomutase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phenylalanine AM
-
phenylalanine aminomutase
-
PATHWAY SOURCE
PATHWAYS
-
-
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).
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
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-phenylalanine
L-beta-phenylalanine
show the reaction diagram
-
-
-
r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3,5-dihydro-5-methylidene-4H-imidazol-4-one
i.e. MIO, essential cofactor
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
0.27 - 0.33
4'-methyl-alpha-phenylalanine
0.022 - 0.93
L-phenylalanine
0.025
styryl-alpha-alanine
mutant L104A, pH 8.5, 31°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
structural determinant that dictates the activity differences between a phenylalanine ammonia lyase (PAL, EC 4.3.1.24) and aminomutase (PAM), overview. An inner loop region closes the active sites of both PAM and PAL. The inner loop is a structural determinant of the lyase and mutase activities of PAM. Three-dimensional structure comparisons of Taxus canadensis PAM with PAM from Taxus chinensis and phenylalanine ammonia lyase from Petroselinum crispum (PcPAL)
additional information
the inner loop is a structural determinant of the lyase and mutase activities of PAM
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PAM_TAXCA
698
0
76532
Swiss-Prot
other Location (Reliability: 2)
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure analysis of TcdPAM, PDB ID 3NZ4
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
PROTEIN VARIANTS
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
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Feng, L.; Wanninayake, U.; Strom, S.; Geiger, J.; Walker, K.
Mechanistic, mutational, and structural evaluation of a taxus phenylalanine aminomutase
Biochemistry
50
2919-2930
2011
Taxus canadensis (Q6GZ04), Taxus canadensis
Manually annotated by BRENDA team
Heberling, M.; Masman, M.; Bartsch, S.; Wybenga, G.; Dijkstra, B.; Marrink, S.; Janssen, D.
Ironing out their differences Dissecting the structural determinants of a phenylalanine aminomutase and ammonia lyase
ACS Chem. Biol.
10
989-997
2015
Taxus chinensis (Q68G84), Taxus canadensis (Q6GZ04)
-
Manually annotated by BRENDA team