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Information on EC 5.4.3.10 - phenylalanine aminomutase (L-beta-phenylalanine forming) and Organism(s) Talaromyces islandicus and UniProt Accession A0A0U1LSP0

for references in articles please use BRENDA:EC5.4.3.10
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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:
Talaromyces islandicus
UNIPROT: A0A0U1LSP0
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Word Map
The taxonomic range for the selected organisms is: Talaromyces islandicus
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-2,3-aminomutase
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-phenylalanine = L-beta-phenylalanine
show the reaction diagram
(R)-selective PAM reaction mechanism, overview
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
L-phenylalanine
L-beta-phenylalanine
show the reaction diagram
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
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
the enzyme belongs to the MIO-dependent aminomutases. Aminomutases (defined as isomerases mediating intramolecular transfer of amino groups) catalyze the synthetically challenging shift of an amine group along a saturated carbon chain, typically of an amino acid. PAMs and tyrosine aminomutases (TAMs) share the same structure, mechanistic pathway, and characteristics of phenylalanine ammonia-lyases (PALs), histidine ammonia-lyases (HALs), and tyrosine ammonia-lyases (TALs), being all members of the same MIO-dependent enzyme family, also called class I lyase-like enzymes
metabolism
phenylalanine aminomutase (PAM) catalyzes the 2,3-shift of the alpha-amino group of L-phenylalanine and L-tyrosine to afford beta-phenylalanine. Biocatalytic strategies for the production of (R)- or (S)-beta-arylalanines employing enzymes with enantiocomplementary aminomutase activity. Metabolites containing (R)-beta-phenylalanine are chemically similar cyclochlorotines from the plant Talaromyces islandicum
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
CCTP_TALIS
997
0
109350
Swiss-Prot
other Location (Reliability: 4)
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Parmeggiani, F
; Weise, N.J.; Ahmed, S.T.; Turner, N.J. Synthetic and therapeutic applications of ammonia-lyases and aminomutases
Chem. Rev.
118
73-118
2018
Aster tataricus, Pelliciarosea asterica, Talaromyces islandicus (A0A0U1LSP0), Taxus chinensis (Q68G84)
Manually annotated by BRENDA team