CBL_CORST
ID CBL_CORST Reviewed; 377 AA.
AC Q64HC5;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 51.
DE RecName: Full=Cysteine-S-conjugate beta-lyase {ECO:0000305|PubMed:17191898};
DE Short=C-S lyase {ECO:0000303|PubMed:17191898};
DE EC=4.4.1.13 {ECO:0000269|PubMed:17191898, ECO:0000269|PubMed:18515361};
DE AltName: Full=Cystathionine beta-lyase {ECO:0000305};
DE Short=CBL;
GN Name=metC {ECO:0000303|PubMed:17191898};
OS Corynebacterium striatum.
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=43770;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBSTRATE SPECIFICITY.
RC STRAIN=Ax20;
RX PubMed=17191898; DOI=10.1002/cbdv.200490079;
RA Natsch A., Schmid J., Flachsmann F.;
RT "Identification of odoriferous sulfanylalkanols in human axilla secretions
RT and their formation through cleavage of cysteine precursors by a C-S lyase
RT isolated from axilla bacteria.";
RL Chem. Biodivers. 1:1058-1072(2004).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=Ax20;
RX PubMed=18515361; DOI=10.1074/jbc.m800730200;
RA Emter R., Natsch A.;
RT "The sequential action of a dipeptidase and a beta-lyase is required for
RT the release of the human body odorant 3-methyl-3-sulfanylhexan-1-ol from a
RT secreted Cys-Gly-(S) conjugate by Corynebacteria.";
RL J. Biol. Chem. 283:20645-20652(2008).
CC -!- FUNCTION: Catalyzes the cleavage of the cysteine-S bond in various
CC cysteine-S-conjugates (PubMed:17191898, PubMed:18515361). Cleaves L-
CC cystathionine, as well as S-substituted cysteine conjugates S-benzyl-L-
CC cysteine and S-ethyl-L-cysteine (PubMed:17191898). Releases four human
CC body odoriferous sulfanylalkanols: 3-methyl-3-sulfanylhexan-1-ol
CC (3M3SH), 3-sulfanylhexan-1-ol, 2-methyl-3-sulfanylbutan-1-ol and 3-
CC sulfanylpentan-1-ol; the release is obtained after the sequential
CC hydrolysis of the Cys-Gly bond of the odorless Cys-Gly-S-conjugate
CC precursors by the dipeptidase TpdA, then the cleavage of the resulting
CC Cys-S-conjugates by MetC (PubMed:17191898, PubMed:18515361).
CC {ECO:0000269|PubMed:17191898, ECO:0000269|PubMed:18515361}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an S-substituted L-cysteine + H2O = a thiol + NH4(+) +
CC pyruvate; Xref=Rhea:RHEA:18121, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:28938, ChEBI:CHEBI:29256, ChEBI:CHEBI:58717; EC=4.4.1.13;
CC Evidence={ECO:0000269|PubMed:17191898, ECO:0000269|PubMed:18515361};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18122;
CC Evidence={ECO:0000305|PubMed:17191898, ECO:0000305|PubMed:18515361};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + S-(1-hydroxy-3-methylhexan-3-yl)-L-cysteine = 3-methyl-
CC 3-sulfanylhexan-1-ol + NH4(+) + pyruvate; Xref=Rhea:RHEA:64740,
CC ChEBI:CHEBI:15361, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:145805, ChEBI:CHEBI:146780;
CC Evidence={ECO:0000269|PubMed:17191898, ECO:0000269|PubMed:18515361};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64741;
CC Evidence={ECO:0000305|PubMed:17191898, ECO:0000305|PubMed:18515361};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + S-3-(hexan-1-ol)-L-cysteine = 3-sulfanyl-1-hexanol +
CC NH4(+) + pyruvate; Xref=Rhea:RHEA:64744, ChEBI:CHEBI:15361,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:77690,
CC ChEBI:CHEBI:156140; Evidence={ECO:0000269|PubMed:17191898};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64745;
CC Evidence={ECO:0000305|PubMed:17191898};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + S-(4-hydroxy-3-methylbutan-2-yl)-L-cysteine = 2-methyl-
CC 3-sulfanylbutan-1-ol + NH4(+) + pyruvate; Xref=Rhea:RHEA:64748,
CC ChEBI:CHEBI:15361, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:156146, ChEBI:CHEBI:156147;
CC Evidence={ECO:0000269|PubMed:17191898};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64749;
CC Evidence={ECO:0000305|PubMed:17191898};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-sulfanylpentan-1-ol-L-cysteine + H2O = 3-sulfanyl-1-pentanol
CC + NH4(+) + pyruvate; Xref=Rhea:RHEA:64752, ChEBI:CHEBI:15361,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:156143,
CC ChEBI:CHEBI:156144; Evidence={ECO:0000269|PubMed:17191898};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64753;
CC Evidence={ECO:0000305|PubMed:17191898};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L,L-cystathionine = L-homocysteine + NH4(+) + pyruvate;
CC Xref=Rhea:RHEA:13965, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:28938, ChEBI:CHEBI:58161, ChEBI:CHEBI:58199;
CC Evidence={ECO:0000269|PubMed:17191898};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13966;
CC Evidence={ECO:0000305|PubMed:17191898};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + S-benzyl-L-cysteine = benzylthiol + NH4(+) + pyruvate;
CC Xref=Rhea:RHEA:64756, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:28938, ChEBI:CHEBI:137674, ChEBI:CHEBI:145803;
CC Evidence={ECO:0000269|PubMed:17191898};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64757;
CC Evidence={ECO:0000305|PubMed:17191898};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + S-ethyl-L-cysteine = ethanethiol + NH4(+) + pyruvate;
CC Xref=Rhea:RHEA:64760, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:28938, ChEBI:CHEBI:46511, ChEBI:CHEBI:156145;
CC Evidence={ECO:0000269|PubMed:17191898};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64761;
CC Evidence={ECO:0000305|PubMed:17191898};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250|UniProtKB:P23256};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.4 mM for cystathionine {ECO:0000269|PubMed:17191898};
CC KM=1.8 mM for (S)-S-benzyl-cysteine {ECO:0000269|PubMed:17191898};
CC -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC aminotransferase family. MalY/PatB cystathionine beta-lyase subfamily.
CC {ECO:0000305}.
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DR EMBL; AY646680; AAU06200.1; -; Genomic_DNA.
DR AlphaFoldDB; Q64HC5; -.
DR SMR; Q64HC5; -.
DR BioCyc; MetaCyc:MON-20504; -.
DR GO; GO:0004121; F:cystathionine beta-lyase activity; IEA:RHEA.
DR GO; GO:0047804; F:cysteine-S-conjugate beta-lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
PE 1: Evidence at protein level;
KW Aminotransferase; Lyase; Pyridoxal phosphate; Transferase.
FT CHAIN 1..377
FT /note="Cysteine-S-conjugate beta-lyase"
FT /id="PRO_0000451212"
FT MOD_RES 223
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P23256"
SQ SEQUENCE 377 AA; 41719 MW; 113B41E2D9229730 CRC64;
MQFSNLDTLR TRGTRKWTQF DDDVIPMFVA ESDFPTAPAI KEAIIDACER EMFGYTPAPH
AHHLGEAVAD FYDWRYGWRP DAAKIFPVAD VVRGVLLAIQ YFTDGDVIVP VPAYFPFLPI
AEAAGRNRID ISSDKGLEGG LDMAEVEEAF KNGAGSIIVT NPFNPGGWMF TSEELDQICD
IARRYKGRVL VDEIHAPLTY GKRHVCAAAN NPDVCITVTA TSKAWNVAGL KCAQMIFTND
EDVKTWNAIN PVAKDGVGTL GIIAAEAAYE SGREHLDWQV EQLKANRDWL VENLPSLIPG
IRFEIPDATY LMFLDFKDTK LGVDKPAAYL LKHARVALSE GVDFGPGGEH RARMNFATSP
EILKEATERI ARAIEVV
