TYRDC_LEVBR
ID TYRDC_LEVBR Reviewed; 626 AA.
AC J7GQ11;
DT 13-NOV-2019, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2012, sequence version 1.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=L-tyrosine decarboxylase {ECO:0000303|PubMed:24211777};
DE Short=TDC {ECO:0000303|PubMed:24211777};
DE EC=4.1.1.25 {ECO:0000269|PubMed:24211777, ECO:0000269|PubMed:27292129};
GN Name=tdc {ECO:0000303|PubMed:24211777, ECO:0000312|EMBL:AFP73381.1};
GN ORFNames=CNR29_12740 {ECO:0000312|EMBL:PBQ24843.1},
GN N624_0219 {ECO:0000312|EMBL:KIO94105.1},
GN UCCLBBS449_2369 {ECO:0000312|EMBL:QCZ54275.1};
OS Levilactobacillus brevis (Lactobacillus brevis).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Levilactobacillus.
OX NCBI_TaxID=1580;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBSTRATE SPECIFICITY, AND
RP SUBUNIT.
RC STRAIN=CGMCC 1.2028;
RX PubMed=24211777; DOI=10.1016/j.pep.2013.10.018;
RA Zhang K., Ni Y.;
RT "Tyrosine decarboxylase from Lactobacillus brevis: Soluble expression and
RT characterization.";
RL Protein Expr. Purif. 94:33-39(2014).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TMW 1.313;
RA Behr J., Preissler P., Geissler A.J., Ehrenreich A., Angelov A.,
RA Vogel R.F.;
RT "Identification of ecotype-specific marker genes for categorization of
RT beer-spoiling Lactobacillus brevis.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D7;
RA Kwon M.-S., Lim S.K., Choi H.-J.;
RT "Genome sequence of Lactobacillus brevis D7.";
RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCCLBBS449;
RA Feyereisen M.;
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0007744|PDB:5HSI, ECO:0007744|PDB:5HSJ}
RP X-RAY CRYSTALLOGRAPHY (1.73 ANGSTROMS) OF APOENZYME AND IN COMPLEX WITH
RP PLP, PYRIDOXAL PHOSPHATE AT LYS-392, FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, MUTAGENESIS OF HIS-241; TYR-398;
RP TYR-420 AND SER-586, AND ACTIVE SITE.
RC STRAIN=CGMCC 1.2028;
RX PubMed=27292129; DOI=10.1038/srep27779;
RA Zhu H., Xu G., Zhang K., Kong X., Han R., Zhou J., Ni Y.;
RT "Crystal structure of tyrosine decarboxylase and identification of key
RT residues involved in conformational swing and substrate binding.";
RL Sci. Rep. 6:27779-27779(2016).
CC -!- FUNCTION: Catalyzes the decarboxylation of L-tyrosine to produce
CC tyramine (PubMed:24211777, PubMed:27292129). Cannot use other aromatic
CC L-amino acids as substrates like L-phenylalanine, L-tryptophan and L-
CC glutamate (PubMed:24211777). {ECO:0000269|PubMed:24211777,
CC ECO:0000269|PubMed:27292129}.
CC -!- FUNCTION: Is also able to decarboxylate the Parkinson's disease
CC medication levodopa (L-dopa) to dopamine in vitro.
CC {ECO:0000269|PubMed:24211777, ECO:0000269|PubMed:27292129}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + L-tyrosine = CO2 + tyramine; Xref=Rhea:RHEA:14345,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:58315,
CC ChEBI:CHEBI:327995; EC=4.1.1.25;
CC Evidence={ECO:0000269|PubMed:24211777, ECO:0000269|PubMed:27292129};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14346;
CC Evidence={ECO:0000305|PubMed:24211777, ECO:0000305|PubMed:27292129};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + L-dopa = CO2 + dopamine; Xref=Rhea:RHEA:12272,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57504,
CC ChEBI:CHEBI:59905; Evidence={ECO:0000269|PubMed:24211777,
CC ECO:0000269|PubMed:27292129};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:24211777};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.59 mM for L-tyrosine {ECO:0000269|PubMed:24211777};
CC KM=0.6 mM for L-tyrosine {ECO:0000269|PubMed:27292129};
CC KM=0.8 mM for L-dopa {ECO:0000269|PubMed:27292129};
CC Vmax=147.1 umol/min/mg enzyme for the decarboxylation of L-tyrosine
CC {ECO:0000269|PubMed:24211777};
CC Note=kcat is 343.1 sec(-1) for the decarboxylation of L-tyrosine
CC (PubMed:24211777). kcat is 124.8 sec(-1) for the decarboxylation of
CC L-tyrosine. kcat is 76.5 sec(-1) for the decarboxylation of L-dopa
CC (PubMed:27292129). {ECO:0000269|PubMed:24211777,
CC ECO:0000269|PubMed:27292129};
CC pH dependence:
CC Optimum pH is 5.0 for the decarboxylation of L-tyrosine. Is not
CC active at pH below 3.5 or above 9.0. More than 90% of activity
CC remains over pH range from 5.0 to 6.0, and activity decreases rapidly
CC at pH below 5.0 or higher than 6.0. {ECO:0000269|PubMed:24211777};
CC Temperature dependence:
CC Optimum temperature is 50 degrees Celsius. Only 8.5% of activity
CC remains at 70 degrees Celsius. However, the enzyme shows poor
CC stability at 50 degrees Celsius, the relative activity dropped to 14%
CC after 1 h of incubation. {ECO:0000269|PubMed:24211777};
CC -!- PATHWAY: Amino-acid metabolism. {ECO:0000305|PubMed:24211777}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:24211777,
CC ECO:0000269|PubMed:27292129}.
CC -!- MISCELLANEOUS: In gut microbiota this enzyme is in fact exclusively
CC responsible for the decarboxylation of levodopa, and thus reduces in
CC situ levels of levodopa in the treatment of Parkinson's disease. It was
CC shown that abundance of bacterial tyrosine decarboxylase in the
CC proximal small intestine - the primary site of levodopa absorption
CC - contributes to interindividual variation in drug efficacy and can
CC explain the requirement for an increased dosage regimen of levodopa
CC treatment in Parkinson's disease patients.
CC {ECO:0000250|UniProtKB:Q838D6}.
CC -!- SIMILARITY: Belongs to the group II decarboxylase family. Tyrosine
CC decarboxylase subfamily. {ECO:0000305}.
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DR EMBL; JX204286; AFP73381.1; -; Genomic_DNA.
DR EMBL; JXUF01000002; KIO94105.1; -; Genomic_DNA.
DR EMBL; NVYO01000001; PBQ24843.1; -; Genomic_DNA.
DR EMBL; CP031198; QCZ54275.1; -; Genomic_DNA.
DR RefSeq; WP_011668784.1; NZ_QQPA01000097.1.
DR PDB; 5HSI; X-ray; 1.73 A; A/B=1-626.
DR PDB; 5HSJ; X-ray; 1.90 A; A/B=1-626.
DR PDBsum; 5HSI; -.
DR PDBsum; 5HSJ; -.
DR AlphaFoldDB; J7GQ11; -.
DR SMR; J7GQ11; -.
DR EnsemblBacteria; KIO94105; KIO94105; N624_0219.
DR EnsemblBacteria; PBQ24843; PBQ24843; CNR29_12740.
DR PATRIC; fig|1580.52.peg.219; -.
DR OMA; ANYEGLW; -.
DR BRENDA; 4.1.1.25; 2851.
DR Proteomes; UP000217918; Unassembled WGS sequence.
DR Proteomes; UP000307074; Chromosome.
DR GO; GO:0036468; F:L-dopa decarboxylase activity; IDA:UniProtKB.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IDA:UniProtKB.
DR GO; GO:0004837; F:tyrosine decarboxylase activity; IDA:UniProtKB.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR Gene3D; 3.40.640.10; -; 1.
DR InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR022397; Tyrosine_deCO2ase_bac.
DR Pfam; PF00282; Pyridoxal_deC; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR TIGRFAMs; TIGR03811; tyr_de_CO2_Ent; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Decarboxylase; Lyase; Pyridoxal phosphate.
FT CHAIN 1..626
FT /note="L-tyrosine decarboxylase"
FT /id="PRO_0000448497"
FT ACT_SITE 420
FT /note="Proton donor"
FT /evidence="ECO:0000305|PubMed:27292129"
FT BINDING 158..159
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000269|PubMed:27292129"
FT BINDING 298
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000269|PubMed:27292129"
FT BINDING 389..391
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000269|PubMed:27292129"
FT BINDING 440
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000269|PubMed:27292129"
FT MOD_RES 392
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000269|PubMed:27292129,
FT ECO:0007744|PDB:5HSJ"
FT MUTAGEN 241
FT /note="H->A: Complete loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:27292129"
FT MUTAGEN 241
FT /note="H->N,Q: Almost complete loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:27292129"
FT MUTAGEN 398
FT /note="Y->A: High decrease in catalytic efficiency."
FT /evidence="ECO:0000269|PubMed:27292129"
FT MUTAGEN 420
FT /note="Y->A,F: Complete loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:27292129"
FT MUTAGEN 586
FT /note="S->A: Increase in catalytic efficiency and substrate
FT affinity."
FT /evidence="ECO:0000269|PubMed:27292129"
FT HELIX 13..16
FT /evidence="ECO:0007829|PDB:5HSI"
FT HELIX 25..45
FT /evidence="ECO:0007829|PDB:5HSI"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:5HSI"
FT HELIX 56..59
FT /evidence="ECO:0007829|PDB:5HSI"
FT HELIX 62..85
FT /evidence="ECO:0007829|PDB:5HSI"
FT TURN 92..94
FT /evidence="ECO:0007829|PDB:5HSI"
FT STRAND 95..98
FT /evidence="ECO:0007829|PDB:5HSI"
FT HELIX 105..115
FT /evidence="ECO:0007829|PDB:5HSI"
FT HELIX 124..126
FT /evidence="ECO:0007829|PDB:5HSI"
FT HELIX 128..144
FT /evidence="ECO:0007829|PDB:5HSI"
FT STRAND 151..157
FT /evidence="ECO:0007829|PDB:5HSI"
FT HELIX 158..182
FT /evidence="ECO:0007829|PDB:5HSI"
FT HELIX 184..187
FT /evidence="ECO:0007829|PDB:5HSI"
FT HELIX 192..195
FT /evidence="ECO:0007829|PDB:5HSI"
FT HELIX 200..209
FT /evidence="ECO:0007829|PDB:5HSI"
FT HELIX 210..213
FT /evidence="ECO:0007829|PDB:5HSI"
FT HELIX 214..219
FT /evidence="ECO:0007829|PDB:5HSI"
FT HELIX 222..224
FT /evidence="ECO:0007829|PDB:5HSI"
FT HELIX 228..231
FT /evidence="ECO:0007829|PDB:5HSI"
FT STRAND 233..237
FT /evidence="ECO:0007829|PDB:5HSI"
FT HELIX 238..240
FT /evidence="ECO:0007829|PDB:5HSI"
FT HELIX 241..250
FT /evidence="ECO:0007829|PDB:5HSI"
FT HELIX 255..257
FT /evidence="ECO:0007829|PDB:5HSI"
FT STRAND 258..261
FT /evidence="ECO:0007829|PDB:5HSI"
FT STRAND 267..269
FT /evidence="ECO:0007829|PDB:5HSI"
FT HELIX 271..283
FT /evidence="ECO:0007829|PDB:5HSI"
FT STRAND 288..296
FT /evidence="ECO:0007829|PDB:5HSI"
FT TURN 298..300
FT /evidence="ECO:0007829|PDB:5HSI"
FT HELIX 306..317
FT /evidence="ECO:0007829|PDB:5HSI"
FT TURN 318..320
FT /evidence="ECO:0007829|PDB:5HSI"
FT STRAND 324..328
FT /evidence="ECO:0007829|PDB:5HSI"
FT TURN 330..332
FT /evidence="ECO:0007829|PDB:5HSI"
FT HELIX 333..339
FT /evidence="ECO:0007829|PDB:5HSI"
FT HELIX 349..351
FT /evidence="ECO:0007829|PDB:5HSI"
FT HELIX 352..358
FT /evidence="ECO:0007829|PDB:5HSI"
FT STRAND 361..364
FT /evidence="ECO:0007829|PDB:5HSI"
FT HELIX 371..378
FT /evidence="ECO:0007829|PDB:5HSI"
FT HELIX 379..382
FT /evidence="ECO:0007829|PDB:5HSI"
FT STRAND 383..387
FT /evidence="ECO:0007829|PDB:5HSI"
FT TURN 390..394
FT /evidence="ECO:0007829|PDB:5HSI"
FT STRAND 401..407
FT /evidence="ECO:0007829|PDB:5HSI"
FT HELIX 408..413
FT /evidence="ECO:0007829|PDB:5HSI"
FT HELIX 432..435
FT /evidence="ECO:0007829|PDB:5HSI"
FT HELIX 443..455
FT /evidence="ECO:0007829|PDB:5HSI"
FT TURN 460..462
FT /evidence="ECO:0007829|PDB:5HSI"
FT HELIX 463..481
FT /evidence="ECO:0007829|PDB:5HSI"
FT STRAND 485..488
FT /evidence="ECO:0007829|PDB:5HSI"
FT STRAND 491..497
FT /evidence="ECO:0007829|PDB:5HSI"
FT STRAND 502..512
FT /evidence="ECO:0007829|PDB:5HSI"
FT HELIX 518..531
FT /evidence="ECO:0007829|PDB:5HSI"
FT STRAND 545..552
FT /evidence="ECO:0007829|PDB:5HSI"
FT HELIX 553..556
FT /evidence="ECO:0007829|PDB:5HSI"
FT TURN 557..560
FT /evidence="ECO:0007829|PDB:5HSI"
FT HELIX 561..566
FT /evidence="ECO:0007829|PDB:5HSI"
FT HELIX 571..577
FT /evidence="ECO:0007829|PDB:5HSI"
FT STRAND 579..586
FT /evidence="ECO:0007829|PDB:5HSI"
FT HELIX 595..618
FT /evidence="ECO:0007829|PDB:5HSI"
SQ SEQUENCE 626 AA; 70507 MW; 88C111F99D259766 CRC64;
MEKSNRSLKD LDLNALFIGD KAENGQLYKD LLNKLVDEHL GWRKNYIPSD PNMIGPEDQN
SPAFKKTVGH MKTVLDQLSE RIRTESVPWH SAGRYWGHMN SETLMPALLA YNYAMLWNGN
NVAYESSPAT SQMEEEVGQE FARLMGYDYG WGHIVADGSL ANLEGLWYAR NIKSLPFAMK
EVNPELVAGK SDWELLNMPT KEIMDLLENA GSQIDEVKKR SARSGKNLQR LGKWLVPQTK
HYSWMKAADI IGIGLDQVVP VPIDSNYRMD IQALESIIRK YAAEKTPILG VVGVAGSTEE
GAVDGIDKIV ALRQKLQKEG IYFYLHVDAA YGGYARALFL DEDDQFIPYK NLQKVHAENH
VFTEDKEYIK PEVYAAYKAF DQAESITIDP HKMGYVPYSA GGIVIQDIRM RDTISYFATY
VFEKGADIPA LLGAYILEGS KAGATAASVW AAHHTLPLNV TGYGKLEGAS IEGAHRYYDF
LKNLKFEVAG KRISVHPLIS PDFNMVDYVL KEDGNDDLIE MNRLNHAFYE QASYVKGSLY
GKEYIVSHTD FAIPDYGDSP LAFVESLGFS EVEWRHAGKV TIIRASVMTP YMNQRENFDY
FAPRIKKAIQ ADLEKVYASV NQKENV
