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Information on EC 4.3.1.25 - phenylalanine/tyrosine ammonia-lyase
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4.3.1.25 phenylalanine/tyrosine ammonia-lyaseIUBMB 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 4.3.1.23 (tyrosine ammonia-lyase) and EC 4.3.1.24 (phenylalanine ammonia-lyase). The enzyme from some monocots, including maize, and from the yeast Rhodosporidium toruloides, deaminate L-phenylalanine and L-tyrosine with similar catalytic efficiency . 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 .
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Word Map
- 4.3.1.25
- synthesis
-
p-hydroxycinnamic
- glutinis
-
deamination
-
rhodotorula
- maize
- hydrolysate
- pharmacology
- food industry
- nutrition
- analysis
- medicine
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
Synonyms
PAL, PAL/TAL, PAL4, phenylalanine-tyrosine ammonia lyase, PTAL, RtPAL, Sb04g026510, Sb06g022740, SbPAL1, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
PAL
PAL/TAL
phenylalanine-tyrosine ammonia lyase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-tyrosine = trans-p-hydroxycinnamate + NH3
-
-
-
-
L-phenylalanine = trans-cinnamate + NH3
-
-
-
-
L-phenylalanine = trans-cinnamate + NH3
ordered uni-bi reaction sequence
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PATHWAY SOURCE
PATHWAYS
MetaCyc
avenanthramide biosynthesis, benzoate biosynthesis II (CoA-independent, non-beta-oxidative), cinnamoyl-CoA biosynthesis, coumarins biosynthesis (engineered), ephedrine biosynthesis, naringenin biosynthesis (engineered), phenylpropanoid biosynthesis, initial reactions, rosmarinic acid biosynthesis I, suberin monomers biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
L-phenylalanine(or L-tyrosine):trans-cinnamate(or trans-p-hydroxycinnamate) ammonia-lyase
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 4.3.1.23 (tyrosine ammonia-lyase) and EC 4.3.1.24 (phenylalanine ammonia-lyase). The enzyme from some monocots, including maize, and from the yeast Rhodosporidium toruloides, deaminate L-phenylalanine and L-tyrosine with similar catalytic efficiency [3]. The enzyme contains the cofactor 3,5-dihydro-5-methylidene-4H-imidazol-4-one (MIO), which is common to this family [3]. This unique cofactor is formed autocatalytically by cyclization and dehydration of the three amino-acid residues alanine, serine and glycine [4].
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-chloro-trans-cinnamate + NH3
2-chloro-L-phenylalanine
51.4% conversion
-
-
?
2-fluoro-trans-cinnamate + NH3
2-fluoro-L-phenylalanine
94.3% conversion
-
-
?
2-hydroxy-trans-cinnamate + NH3
2-hydroxy-L-phenylalanine
15.7% conversion
-
-
?
2-methoxy-trans-cinnamate + NH3
2-methoxy-L-phenylalanine
64.9% conversion
-
-
?
3-chloro-trans-cinnamate + NH3
3-chloro-L-phenylalanine
71.6% conversion
-
-
?
3-fluoro-trans-cinnamate + NH3
3-fluoro-L-phenylalanine
61.5% conversion
-
-
?
3-hydroxy-trans-cinnamate + NH3
3-hydroxy-L-phenylalanine
30.3% conversion
-
-
?
3-methoxy-4-hydroxy-trans-cinnamate + NH3
3-methoxy-4-hydroxy-L-phenylalanine
60.3% conversion
-
-
?
3-methoxy-trans-cinnamate + NH3
3-methoxy-L-phenylalanine
77.8% conversion
-
-
?
4-fluoro-trans-cinnamate + NH3
4-fluoro-L-phenylalanine
57.5% conversion
-
-
?
4-hydroxy-trans-cinnamate + NH3
4-hydroxy-L-phenylalanine
61.1% conversion
-
-
?
4-methoxy-trans-cinnamate + NH3
4-methoxy-L-phenylalanine
0.7% conversion
-
-
?
L-tyrosine methyl ester
4-hydroxycinnamic acid methyl ester + NH3
-
-
-
-
?
L-phenylalanine
trans-cinnamate + NH3
key gateway enzyme linking the phenylpropanoid secondary pathway to primary metabolism
-
-
r
L-phenylalanine
trans-cinnamate + NH3
the bifunctional enzyme shows KM-values for L-Phe and L-Tyr in the same order of magnitude
-
-
r
L-phenylalanine
trans-cinnamate + NH3
enzyme of the phenylpropanoid pathway
-
-
?
L-tyrosine
p-coumarate + NH3
-
substrate binding is cooperative, nH 2.6
-
-
?
L-tyrosine
trans-p-hydroxycinnamate + NH3
the bifunctional enzyme shows KM-values for L-Phe and L-Tyr in the same order of magnitude
-
-
?
additional information
?
-
wild type enzyme and mutants show no catalytic activity with His
-
-
?
additional information
?
-
wild type enzyme and mutants show no catalytic activity with His
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-phenylalanine
trans-cinnamate + NH3
key gateway enzyme linking the phenylpropanoid secondary pathway to primary metabolism
-
-
r
L-phenylalanine
trans-cinnamate + NH3
enzyme of the phenylpropanoid pathway
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3,5-dihydro-5-methylidene-4H-imidazol-4-one
the cofactor is regenerated during the reaction cycle and thus does not require external cofactor regeneration
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
m-cresol/glycine
-
0.387 mM, 50% inhibition, strong synergistic inhibition
o-cresol/glycine
-
0.078 mM, 50% inhibition, strong synergistic inhibition
CN-
-
the substrate analog DL-2-hydroxyphenylalanine or cinnamate protects
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.5
8.8
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
enzyme expression is induced up to 3fold by presence of L-isoleucine, L-phenylalanine or L-tyrosine in growth medium. The presence of trans-cinnamic acid suppresses enzyme expression
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
in shoot and branch shoot, mainly loclaized to sclerenchymal cells
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
metabolism
key gateway enzyme linking the phenylpropanoid secondary pathway to primary metabolism
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PALY_MAIZE
703
0
74927
Swiss-Prot
other Location (Reliability: 4)
PALY_RHOTO
716
0
76880
Swiss-Prot
other Location (Reliability: 3)
C5XXT8_SORBI
704
0
75602
TrEMBL
other Location (Reliability: 5)
C5YCD6_SORBI
703
0
75699
TrEMBL
other Location (Reliability: 4)
D5KS97_BAMOL
701
0
75711
TrEMBL
other Location (Reliability: 2)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
R123A
modest improvements in resistance against protease inactivation
R123H
modest improvements in resistance against protease inactivation
R123Q
modest improvements in resistance against protease inactivation
Y110A
modest improvements in resistance against protease inactivation
Y110H
modest improvements in resistance against protease inactivation
Y110L
modest improvements in resistance against protease inactivation
F102Y
the turnover rate for L-Tyr is improved 3.6fold, whereas the turnover rate for L-Phe is unaffected. Km values for both L-Tyr and L-Phe are increased by 7.6- and 24fold, respectively, which causes reduced enzyme efficiency for both substrates
H123F
the mutant shows 6.2fold elevation in catalytic efficiency (kcat/Km) for L-Phe, mainly due to a 5.7fold decrease in Km. The mutant enzyme loses activity for L-Tyr. The loss of polarity in the H123F mutant orients both L-Tyr and L-Phe in similar positions, where the ortho-carbon is closer to the methylidene carbon of 4-methylidene-imidazole-5-one
H123Y
the catalytic efficiency of the mutant enzyme for L-Phe is reduced, mainly due to a 10fold decrease in the turnover rate. The H123Y mutant also loses activity against L-Tyr
K443E
the mutant enzyme shows no measurable activity against any of the three substrates, L-Phe, L-Tyr, and L-His
Y96F
the mutant enzyme displays only trace amounts of activity for both L-Tyr and L-Phe
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
0-2°C, 50 mM Tris/HCl, 0.01% Mn2+, pH 8.8, whole cells retain 85% of initial enzyme activity for at least 12 weeks
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
controlled expression in Escherichia coli to mitigate product toxicity
expression in Escherichia coli
controlled expression in Escherichia coli to mitigate product toxicity
-
controlled expression in Escherichia coli to mitigate product toxicity
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
-
rapid quantization of Phe and Tyr in plasma and serum from subjects with phenylketonuria
food industry
medicine
enzyme substitution therapy for the treatment of phenylketonuria
nutrition
pharmacology
synthesis
food industry
the enzyme is a useful biocatalyst for removal of L-phenylalanine from protein hydrolysates, which can be evaluated as potential ingredients in foodstuffs for phenylketonuria patients. The enzyme is also capable to catalyze the deamination of L-tyrosine to p-coumaric acid but at a substantially low reaction rate. Therefore, the final content of L-Tyr in samples treated with L-phenylalanine ammonia-lyase should be analyzed in each case and taken in consideration to avoid its deficiency in phenylketonuria patients
food industry
Rhodotorula toruloides NBRC 0559
-
the enzyme is a useful biocatalyst for removal of L-phenylalanine from protein hydrolysates, which can be evaluated as potential ingredients in foodstuffs for phenylketonuria patients. The enzyme is also capable to catalyze the deamination of L-tyrosine to p-coumaric acid but at a substantially low reaction rate. Therefore, the final content of L-Tyr in samples treated with L-phenylalanine ammonia-lyase should be analyzed in each case and taken in consideration to avoid its deficiency in phenylketonuria patients
-
nutrition
the enzyme is a useful biocatalyst for removal of L-phenylalanine from protein hydrolysates, which can be evaluated as potential ingredients in foodstuffs for phenylketonuria patients. The enzyme is also capable to catalyze the deamination of L-tyrosine to p-coumaric acid but at a substantially low reaction rate. Therefore, the final content of L-Tyr in samples treated with L-phenylalanine ammonia-lyase should be analyzed in each case and taken in consideration to avoid its deficiency in phenylketonuria patients
nutrition
Rhodotorula toruloides NBRC 0559
-
the enzyme is a useful biocatalyst for removal of L-phenylalanine from protein hydrolysates, which can be evaluated as potential ingredients in foodstuffs for phenylketonuria patients. The enzyme is also capable to catalyze the deamination of L-tyrosine to p-coumaric acid but at a substantially low reaction rate. Therefore, the final content of L-Tyr in samples treated with L-phenylalanine ammonia-lyase should be analyzed in each case and taken in consideration to avoid its deficiency in phenylketonuria patients
-
pharmacology
enzyme substitution therapy for the treatment of phenylketonuria
pharmacology
the enzyme is a useful biocatalyst for removal of L-phenylalanine from protein hydrolysates, which can be evaluated as potential ingredients in foodstuffs for phenylketonuria patients. The enzyme is also capable to catalyze the deamination of L-tyrosine to p-coumaric acid but at a substantially low reaction rate. Therefore, the final content of L-Tyr in samples treated with L-phenylalanine ammonia-lyase should be analyzed in each case and taken in consideration to avoid its deficiency in phenylketonuria patients
pharmacology
Rhodotorula toruloides NBRC 0559
-
the enzyme is a useful biocatalyst for removal of L-phenylalanine from protein hydrolysates, which can be evaluated as potential ingredients in foodstuffs for phenylketonuria patients. The enzyme is also capable to catalyze the deamination of L-tyrosine to p-coumaric acid but at a substantially low reaction rate. Therefore, the final content of L-Tyr in samples treated with L-phenylalanine ammonia-lyase should be analyzed in each case and taken in consideration to avoid its deficiency in phenylketonuria patients
-
synthesis
-
immobilization of Escherichia coli cells stably expressing the enzyme on calcium alginate beads for use in batch coversion of L-tyrosine to p-hydroxycinnamic acid. Immobilization and controlling of pH value to 9.8 results in stabilization. In 1 l batch reactions, 50 g/l tyrosine can be converted to 39 g/l p-hydroxycinnamic acid
synthesis
-
use of enzyme for synthesis of optically pure L-phenylalanine from trans-cinnamate
synthesis
reconstructed phenylpropanoid pathway in engineered Escherichia coli or Saccharomyces cerevisiae leads to the biosynthesis of a wide range of phenylpropanoid-derived compounds, including pinocembrin, naringenin, styrene, 2',4',6'-trihydroxydihydrochalcone, trans-resveratrol, trans-cinnamic acid, p-coumarate, p-hydroxystyrene
synthesis
-
synthesis of p-hydroxycinnamic acid methyl ester, which shows antibacterial activity
synthesis
-
use of enzyme for synthesis of optically pure L-phenylalanine from trans-cinnamate
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Camm, E.L.; Towers, G.H.N.
Phenylalanine ammonia lyase
Phytochemistry
12
961-973
1973
Sporidiobolus pararoseus, Triticum aestivum
-
brenda
Hanson, K.R.; Havir, E.A.
Phenylalanine ammonia-lyase
Biochem. Plants
7
577-625
1981
Rhodotorula glutinis
-
brenda
Jorrin, J.; Lopez-Valbuena, R.; Tena, M.
Purification and properties of phenylalanine ammonia-lyase from sunflower (Helianthus annuus L.) hypocotyls
Biochim. Biophys. Acta
964
73-82
1988
Helianthus annuus
-
brenda
Abell, C.W.; Shen, R.S.
Phenylalanine ammonia-lyase from the yeast Rhodotorula glutinis
Methods Enzymol.
142
242-249
1987
Rhodotorula glutinis
brenda
Fritz, R.R.; Hodgins, D.S.; Abell, C.W.
Phenylalanine ammonia-lyase. Induction and purification from yeast and clearance in mammals
J. Biol. Chem.
251
4646-4650
1976
Rhodotorula glutinis
brenda
Jangaard, N.O.
The characterization of phenylalanine ammonia-lyase from several plant species
Phytochemistry
13
1765-1768
1974
Cyperus rotundus, Echinochloa crus-galli, Glycine max, Sorghum halepense, Zea mays
-
brenda
Parkhurst, J.R.; Hodgins, D.S.
Yeast phenylalanine ammonia-lyase. Properties of the enzyme from Sporobolomyces pararoseus and its catalytic site
Arch. Biochem. Biophys.
152
597-605
1972
Sporidiobolus pararoseus
brenda
Hodgins, D.S.
Properties of yeast L-phenylalanine ammonia-lyase
Arch. Biochem. Biophys.
149
91-96
1972
Rhodotorula glutinis
brenda
Vance, C.P.; Bandoni, R.J.; Towers, G.H.N.
Further observations on phenylalanine ammonia-lyase in fungi
Phytochemistry
14
1513-1514
1975
Nectria cinnabarina
-
brenda
Adachi, O.; Matsushita, K.; Shinagawa, E.; Ameyama, M.
Crystallization and properties of L-phenylalanine ammonia-lyase from Rhodosporidium toruloides
Agric. Biol. Chem.
54
2839-2843
1990
Rhodotorula toruloides
-
brenda
Dahiya, J.S.
Isolation and characterization of phenylalanine ammonia-lyase enzyme from the fungus Leptosphaeria maculans
Indian J. Exp. Biol.
31
874-877
1993
Leptosphaeria maculans
-
brenda
Alunni, S.; Cipiciani, A.; Fioroni, G.; Ottavi, L.
Mechanisms of inhibition of phenylalanine ammonia-lyase by phenol inhibitors and phenol/glycine synergistic inhibitors
Arch. Biochem. Biophys.
412
170-175
2003
Rhodotorula glutinis
brenda
Khan, W.; Prithiviraj, B.; Smith, D.L.
Chitosan and chitin oligomers increase phenylalanine ammonia-lyase and tyrosine ammonia-lyase activities in soybean leaves
J. Plant Physiol.
160
859-863
2003
Glycine max
brenda
Trotman, R.J.; Camp, C.E.; Ben-Bassat, A.; DiCosimo, R.; Huang, L.; Crum, G.A.; Sariaslani, F.S.; Haynie, S.L.
Calcium alginate bead immobilization of cells containing tyrosine ammonia lyase activity for use in the production of p-hydroxycinnamic acid
Biotechnol. Prog.
23
638-644
2007
Rhodotorula glutinis
brenda
Vannelli, T.; Xue, Z.; Breinig, S.; Qi, W.W.; Sariaslani, F.S.
Functional expression in Escherichia coli of the tyrosine-inducible tyrosine ammonia-lyase enzyme from yeast Trichosporon cutaneum for production of p-hydroxycinnamic acid
Enzyme Microb. Technol.
41
413-422
2007
Cutaneotrichosporon cutaneum
-
brenda
Xue, Z.; McCluskey, M.; Cantera, K.; Ben-Bassat, A.; Sariaslani, F.S.; Huang, L.
Improved production of p-hydroxycinnamic acid from tyrosine using a novel thermostable phenylalanine/tyrosine ammonia lyase enzyme
Enzyme Microb. Technol.
42
58-64
2007
Phanerochaete chrysosporium, Rhodotorula glutinis
-
brenda
Wall, M.J.; Quinn, A.J.; DCunha, G.B.
Manganese (Mn2+)-dependent storage stabilization of Rhodotorula glutinis phenylalanine ammonia-lyase activity
J. Agric. Food Chem.
56
894-902
2008
Rhodotorula glutinis
brenda
Verhoef, S.; Ballerstedt, H.; Volkers, R.J.; de Winde, J.H.; Ruijssenaars, H.J.
Comparative transcriptomics and proteomics of p-hydroxybenzoate producing Pseudomonas putida S12: novel responses and implications for strain improvement
Appl. Microbiol. Biotechnol.
87
679-690
2010
Pseudomonas putida, Pseudomonas putida S12
brenda
Hsieh, L.S.; Ma, G.J.; Yang, C.C.; Lee, P.D.
Cloning, expression, site-directed mutagenesis and immunolocalization of phenylalanine ammonia-lyase in Bambusa oldhamii
Phytochemistry
71
1999-2009
2010
Bambusa oldhamii (D5KS97)
brenda
MacDonald, M.C.; Arivalagan, P.; Barre, D.E.; MacInnis, J.A.; DCunha, G.B.
Rhodotorula glutinis phenylalanine/tyrosine ammonia lyase enzyme catalyzed synthesis of the methyl ester of para-hydroxycinnamic acid and its potential antibacterial activity
Front. Microbiol.
7
281
2016
Rhodotorula glutinis
brenda
Dressen, A.; Hilberath, T.; Mackfeld, U.; Billmeier, A.; Rudat, J.; Pohl, M.
Phenylalanine ammonia lyase from Arabidopsis thaliana (AtPAL2) A potent MIO-enzyme for the synthesis of non-canonical aromatic alpha-amino acids Part I Comparative characterization to the enzymes from Petroselinum crispum (PcPAL1) and Rhodosporidium to the enzymes from Petroselinum crispum (PcPAL1) and Rhodosporidium toruloides (RtPAL)
J. Biotechnol.
258
148-157
2017
Rhodotorula toruloides (P11544)
brenda
Castaneda, M.T.; Adachi, O.; Hours, R.A.
Reduction of L-phenylalanine in protein hydrolysates using L-phenylalanine ammonia-lyase from Rhodosporidium toruloides
J. Ind. Microbiol. Biotechnol.
42
1299-1307
2015
Rhodotorula toruloides (P11544), Rhodotorula toruloides, Rhodotorula toruloides NBRC 0559 (P11544)
brenda
Jun, S.Y.; Sattler, S.A.; Cortez, G.S.; Vermerris, W.; Sattler, S.E.; Kang, C.
Biochemical and structural analysis of substrate specificity of a phenylalanine ammonia-lyase
Plant Physiol.
176
1452-1468
2018
Sorghum bicolor (C5XXT8), Sorghum bicolor (C5YCD6)
brenda
Kong, J.
Phenylalanine ammonia-lyase, a key component used for phenylpropanoids production by metabolic engineering
RSC Adv.
5
62587-62603
2015
Rhodotorula toruloides (P11544)
-
brenda
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