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Information on EC 4.3.1.23 - tyrosine ammonia-lyase and Organism(s) Cereibacter sphaeroides and UniProt Accession Q3IWB0

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EC Tree
     4 Lyases
         4.3 Carbon-nitrogen lyases
             4.3.1 Ammonia-lyases
                4.3.1.23 tyrosine ammonia-lyase
IUBMB Comments
This enzyme is a member of the aromatic amino acid lyase family, other members of which are EC 4.3.1.3 (histidine ammonia-lyase), EC 4.3.1.24 (phenylalanine ammonia-lyase) and EC 4.3.1.25 (phenylalanine/tyrosine ammonia-lyase). The enzyme contains the cofactor 3,5-dihydro-5-methylidene-4H-imidazol-4-one (MIO), which is common to this family . This unique cofactor is formed autocatalytically by cyclization and dehydration of the three amino-acid residues alanine, serine and glycine . The enzyme is far more active with tyrosine than with phenylalanine as substrate, but the substrate specificity can be switched by mutation of a single amino acid (H89F) in the enzyme from the bacterium Rhodobacter sphaeroides [1,2].
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Cereibacter sphaeroides
UNIPROT: Q3IWB0
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The taxonomic range for the selected organisms is: Cereibacter sphaeroides
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
tyrosine ammonia lyase, tyrosine ammonia-lyase, rstal, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tyrosine ammonia lyase
-
-
tyrosine ammonia-lyase
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -
SYSTEMATIC NAME
IUBMB Comments
L-tyrosine ammonia-lyase (trans-p-hydroxycinnamate-forming)
This enzyme is a member of the aromatic amino acid lyase family, other members of which are EC 4.3.1.3 (histidine ammonia-lyase), EC 4.3.1.24 (phenylalanine ammonia-lyase) and EC 4.3.1.25 (phenylalanine/tyrosine ammonia-lyase). The enzyme contains the cofactor 3,5-dihydro-5-methylidene-4H-imidazol-4-one (MIO), which is common to this family [1]. This unique cofactor is formed autocatalytically by cyclization and dehydration of the three amino-acid residues alanine, serine and glycine [3]. The enzyme is far more active with tyrosine than with phenylalanine as substrate, but the substrate specificity can be switched by mutation of a single amino acid (H89F) in the enzyme from the bacterium Rhodobacter sphaeroides [1,2].
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-tyrosine
trans-p-hydroxycinnamate + NH3
show the reaction diagram
L-phenylalanine
(E)-cinnamate + NH3
show the reaction diagram
-
-
-
-
?
L-tyrosine
trans-p-hydroxycinnamate + NH3
show the reaction diagram
-
-
-
-
?
L-tyrosinol
?
show the reaction diagram
-
-
-
-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.7
L-phenylalanine
-
-
0.1
L-tyrosine
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.6
L-phenylalanine
-
-
0.9
L-tyrosine
-
-
0.12
L-tyrosinol
-
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.226
L-phenylalanine
-
-
10
L-tyrosine
-
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Streptomyces lividans
Synechocystis PCC 6803 expressing tyrosine ammonia-lyase from Rhodobacter sphaeroides under Ptrc1O promoter produce p-coumaric acid at a rate three times higher than that under Ptrc1Ocore promoter
expression in Streptomyces mobaraense
-
overexpression in Arabidopsis thaliana
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
synthesis
-
by expressing Rhodobacter sphaeroides tyrosine ammonia lyase, in Streptomyces mobaraense, which permits the synthesis of p-coumaric acid from glucose, a strain is obtained that produces high amounts of 4-vinylphenol
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Bartsch, S.; Bornscheuer, U.T.
A single residue influences the reaction mechanism of ammonia lyases and mutases
Angew. Chem. Int. Ed. Engl.
48
3362-3365
2009
Cereibacter sphaeroides
Manually annotated by BRENDA team
Nishiyama, Y.; Yun, C.S.; Matsuda, F.; Sasaki, T.; Saito, K.; Tozawa, Y.
Expression of bacterial tyrosine ammonia-lyase creates a novel p-coumaric acid pathway in the biosynthesis of phenylpropanoids in Arabidopsis
Planta
232
209-218
2010
Cereibacter sphaeroides
Manually annotated by BRENDA team
Pinto, G.P.; Ribeiro, A.J.; Ramos, M.J.; Fernandes, P.A.; Toscano, M.; Russo, N.
New insights in the catalytic mechanism of tyrosine ammonia-lyase given by QM/MM and QM cluster models
Arch. Biochem. Biophys.
582
107-115
2015
Cereibacter sphaeroides (Q3IWB0), Cereibacter sphaeroides ATCC 17023 (Q3IWB0)
Manually annotated by BRENDA team
Noda, S.; Kawai, Y.; Tanaka, T.; Kondo, A.
4-Vinylphenol biosynthesis from cellulose as the sole carbon source using phenolic acid decarboxylase- and tyrosine ammonia lyase-expressing Streptomyces lividans
Biores. Technol.
180
59-65
2015
Cereibacter sphaeroides (Q3IWB0)
Manually annotated by BRENDA team
Fujiwara, R.; Noda, S.; Kawai, Y.; Tanaka, T.; Kondo, A.
4-Vinylphenol production from glucose using recombinant Streptomyces mobaraense expressing a tyrosine ammonia lyase from Rhodobacter sphaeroides
Biotechnol. Lett.
38
1543-1549
2016
Cereibacter sphaeroides
Manually annotated by BRENDA team
Tantong, S.; Nuengchamnong, N.; Kumphune, S.; Incharoensakdi, A.; Lindblad, P.; Sirikantaramas, S.
Synechocystis PCC 6803 cells heterologously expressing bacterial tyrosine ammonia lyase can use exogenous tyrosine for p-coumaric acid production
J. Plant Biochem. Biotechnol.
27
118-122
2018
Cereibacter sphaeroides (Q3IWB0)
-
Manually annotated by BRENDA team