KEGG   ENZYME: 4.2.1.22Help
Entry
EC 4.2.1.22                 Enzyme                                 

Name cystathionine beta-synthase;
serine sulfhydrase;
beta-thionase;
methylcysteine synthase;
cysteine synthase;
serine sulfhydrylase;
L-serine hydro-lyase (adding homocysteine)
Class Lyases;
Carbon-oxygen lyases;
Hydro-lyases
BRITE hierarchy
Sysname L-serine hydro-lyase (adding homocysteine; L-cystathionine-forming)
Reaction(IUBMB) L-serine + L-homocysteine = L-cystathionine + H2O [RN:R01290]
Reaction(KEGG) R01290;
(other) R00891 R01289 R04942
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Substrate L-serine [CPD:C00065];
L-homocysteine [CPD:C00155]
Product L-cystathionine [CPD:C02291];
H2O [CPD:C00001]
Cofactor Pyridoxal phosphate [CPD:C00018]
Comment A pyridoxal-phosphate protein. A multifunctional enzyme: catalyses
beta-replacement reactions between L-serine, L-cysteine, cysteine
thioethers, or some other beta-substituted alpha-L-amino acids, and
a variety of mercaptans.
Pathway PATH: ec00260  Glycine, serine and threonine metabolism
PATH: ec00270  Cysteine and methionine metabolism
PATH: ec00450  Selenoamino acid metabolism
PATH: ec01100  Metabolic pathways
Orthology KO: K01697  cystathionine beta-synthase
Genes HSA: 875(CBS)
PTR: 736626(CBS)
MMU: 12411(Cbs)
RNO: 24250(Cbs)
CFA: 611071(CBS)
BTA: 514525(CBS)
ECB: 100057612 100146156
MDO: 100024374
OAA: 100080879
GGA: 418544 418545(CBS)
TGU: 100222166 100225076
XLA: 380308(cbs-a) 446655(cbs-b)
XTR: 493533(TTpA004o05.1)
DRE: 266987(cbsb) 550524(cbsa)
BFO: BRAFLDRAFT_117945
CIN: 100180445
SPU: 591266
DME: Dmel_CG1753
DPO: Dpse_GA14544
DAN: Dana_GF21711
DER: Dere_GG19705
DPE: Dper_GL16398
DSE: Dsec_GM23059
DSI: Dsim_GD17507
DYA: Dyak_GE17904
DGR: Dgri_GH22312
DMO: Dmoj_GI22982
AGA: AgaP_AGAP000162
AAG: AaeL_AAEL008467 AaeL_AAEL008468
CQU: CpipJ_CPIJ012753
AME: 551341(Cbs)
NVI: 100115316
TCA: 656954
API: 100166111
ISC: IscW_ISCW013852
CEL: F54A3.4 ZC373.1
CBR: CBG01937
BMY: Bm1_32965
SMM: Smp_125070.1 Smp_125070.2
NVE: NEMVE_v1g204029
HMG: 100209141
TAD: TRIADDRAFT_30632
CME: CMS037C
SCE: YGR155W(CYS4)
AGO: AGOS_AGR012C
KLA: KLLA0F09317g
LTH: KLTH0D04092g
DHA: DEHA0C15708g
PIC: PICST_77227(CYS4)
PPA: PAS_chr2-2_0137
VPO: Kpol_1026p13
LEL: LELG_01590
ZRO: ZYRO0G07128g
CAL: CaO19.12011
CTP: CTRG_04593
CDU: CD36_01710
CGR: CAGL0E03157g
YLI: YALI0E09108g
NCR: NCU08216
PAN: PODANSg4727
MGR: MGG_07384
FGR: FG06544.1
ANI: AN5820.2
AFM: AFUA_2G07620
AOR: AO090011000931
ANG: An05g00160
AFV: AFLA_047240
PCS: Pc13g05320
NFI: NFIA_083350
CIM: CIMG_00957
URE: UREG_00902
SSL: SS1G_08916
BFU: BC1G_10936
CNE: CNA06170
CNB: CNBA5980
LBC: LACBIDRAFT_171213
MPR: MPER_15900
UMA: UM02792.1
MBR: MONBRDRAFT_14886
DDI: DDB_0191292(cysB)
TGO: TGME49_059180
TET: TTHERM_00558300
PTM: GSPATT00013222001 GSPATT00016616001
TBR: Tb11.02.5400
TCR: 506905.50 508175.360 508177.110 508177.120 508241.140 509149.9
     510381.10 511691.10 511691.20
LMA: LmjF17.0250(CYSB)
LIF: LinJ17.0280
LBZ: LbrM17_V2.0230
PTI: PHATRDRAFT_42003(Cbs)
YEN: YE1470(uptG)
ECA: ECA4113
PCT: PC1_3903
PLU: plu0524
PAY: PAU_00518(mtcB)
ENT: Ent638_1770
ESA: ESA_02767
CTU: Ctu_11050
KPN: KPN_03409
KPE: KPK_0709
KPU: KP1_4684
CKO: CKO_01706
SPE: Spro_1627
PMR: PMI0235
ETR: ETAE_1928(uptG)
HDE: HDEF_1873(cysK)
DDC: Dd586_1871
XFA: XF0603
XFT: PD1548(cysM)
XFM: Xfasm12_1704
XFN: XfasM23_1633
XCC: XCC0597(cysB)
XCB: XC_3636
XCA: xccb100_3753
XCV: XCV3726
XAC: XAC3603(cysB)
XOO: XOO0777(cysB)
XOM: XOO_0707
XOP: PXO_03155(cysB)
SML: Smlt0616(cbsB)
SMT: Smal_0488
PAE: PA0399
PAU: PA14_05220
PAP: PSPA7_0499
PAG: PLES_03971
PFO: Pfl01_3248
PFS: PFLU3406
ILO: IL0218(cysM)
CBS: COXBURSA331_A0059
CBD: CBUD_2125
CBG: CbuG_2033
CBC: CbuK_2075
FTU: FTT_1287(cbs)
FTF: FTF1287(cbs)
FTL: FTL_1174
FTH: FTH_1148(cysK)
FTN: FTN_1302(cysK)
KKO: Kkor_1767
CVI: CV_3395(cysB2)
BMA: BMA1621
BMV: BMASAVP1_A2123
BML: BMA10229_A3191
BMN: BMA10247_1397
BPS: BPSL2215
BPM: BURPS1710b_2647
BPL: BURPS1106A_2561
BPD: BURPS668_2508
BTE: BTH_I1970 BTH_II1370
BGL: bglu_1g23070
POL: Bpro_2830
BBA: Bd3796
ADE: Adeh_3300 Adeh_3706
ACP: A2cp1_3442 A2cp1_3846
AFW: Anae109_3846
ANK: AnaeK_3378 AnaeK_3763
MXA: MXAN_2041
SCL: sce0438 sce8782(cysB)
HOH: Hoch_5286
MLO: mll4505
RET: RHE_CH01775(cysK2)
RHI: NGR_a00730 NGR_b03540
BBT: BBta_0633
RPA: RPA2356
RPT: Rpal_2600
CAK: Caul_4907
PZU: PHZ_c0071
RRU: Rru_A0787
RCE: RC1_1987(cbs)
MAG: amb1847
MTU: Rv1077(cbs)
MTC: MT1108
MRA: MRA_1087(cbs)
MTF: TBFG_11095
MTB: TBMG_02910(TBMG_02910.1)
MBO: Mb1106(cbs)
MBB: BCG_1135(cbs)
MBT: JTY_1108(cbs)
MLE: ML2396(cysM2)
MLB: MLBr_02396(cysM2)
MPA: MAP1024(cysM2)
MAV: MAV_1201
MSM: MSMEG_5270
MUL: MUL_0203(cbs)
MVA: Mvan_4674
MGI: Mflv_2043
MAB: MAB_1195
MMC: Mmcs_4149
MKM: Mkms_4224
MJL: Mjls_4380
MMI: MMAR_4390(cbs)
CJK: jk1981(cysY)
CKP: ckrop_0828
NFA: nfa48320
RHA: RHA1_ro05843
RER: RER_42660(cbs)
ROP: ROP_59040(cbs)
GBR: Gbro_1617
SCO: SCO3077(SCE25.18c)
SMA: SAV_3510(cysM1)
SGR: SGR_4452
LXX: Lxx17700(cysM2)
CMI: CMM_0872(cysB)
CMS: CMS_0127
ART: Arth_3062
AAU: AAur_3038
ACH: Achl_2762
RSA: RSal33209_0896
KRH: KRH_16340
MLU: Mlut_17600
BCV: Bcav_1054
XCE: Xcel_2671
PAC: PPA1290 PPA2278
NCA: Noca_0939
TFU: Tfu_0438
TCU: Tcur_1048
SRO: Sros_3752 Sros_8566
FRA: Francci3_0375
FRE: Franean1_6424
FAL: FRAAL0784(cysM)
NML: Namu_4422
KRA: Krad_1082
SEN: SACE_0899(cysM2)
SVI: Svir_31890
AMI: Amir_0700
STP: Strop_0912
SAQ: Sare_0855
CAI: Caci_0644
BLO: BL1156(cbsSV)
BLJ: BLD_0914(cysK)
BLN: Blon_2004
BAD: BAD_0490(cbsSV)
BLA: BLA_1096(cbsSV)
BLC: Balac_0564
BLT: Balat_0564
SRU: SRU_1123
CPI: Cpin_3667
PHE: Phep_1434
GFO: GFO_2397
FJO: Fjoh_1927
FPS: FP1196
FBA: FIC_00717 FIC_01300
COC: Coch_1829
RBI: RB2501_10222 RB2501_15549
GAU: GAU_3907(cbs)
AVA: Ava_4156
CTE: CT1921
CPC: Cpar_0287
CCH: Cag_1634
CPB: Cphamn1_2178
CLI: Clim_2126
PLT: Plut_0281
PPH: Ppha_2553
PAA: Paes_1945
HAU: Haur_3718
STI: Sthe_2024
MBN: Mboo_1990
MPL: Mpal_1157
APE: APE_1223.1 APE_1586(cysK)
Taxonomy
Structures PDB: 1JBQ  1M54  
Reference
  Authors

  Title

  Journal
  Organism
1  [PMID:5121611]
Braunstein AE, Goryachenkova EV, Tolosa EA, Willhardt IH, Yefremova
LL.
Specificity and some other properties of liver serine sulphhydrase:
evidence for its identity with cystathionine  -synthase.
Biochim. Biophys. Acta. 242 (1971) 247-60.
Gallus gallus [GN:gga]
Reference
  Authors
  Title


  Journal
  Organism
2  [PMID:5672136]
Nakagawa H, Kimura H.
Purification and properties of cystathionine synthetase synthetase
from rat liver: separation of cystathionine synthetase from serine
dehydratase.
Biochem. Biophys. Res. Commun. 32 (1968) 209-14.
Rattus norvegicus [GN:rno]
Reference
  Authors
  Title

  Journal
  Organism
3  [PMID:13991884]
SCHLOSSMANN K, BRUEGGEMANN J, LYNEN F.
[Biosynthesis of cysteine. I. Detection and isolation of serine
sulfhydrase from baker's yeast.]
Biochem. Z. 336 (1962) 258-73.
Saccharomyces cerevisiae [GN:sce]
Other DBs ExplorEnz - The Enzyme Database: 4.2.1.22
IUBMB Enzyme Nomenclature: 4.2.1.22
ExPASy - ENZYME nomenclature database: 4.2.1.22
BRENDA, the Enzyme Database: 4.2.1.22
CAS: 9023-99-8

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