Entry
Name
pyridinium-3,5-bisthiocarboxylic acid mononucleotide synthase;
LarE;
P2CMN sulfurtransferase;
pyridinium-3,5-biscarboxylic acid mononucleotide sulfurtransferase;
P2TMN synthase
Class
Lyases;
Carbon-sulfur lyases;
Carbon-sulfur lyases (only sub-subclass identified to date)
BRITE hierarchy
Sysname
[LarE]-S-[1-(5-O-phosphono-beta-D-ribofuranosyl)-5-(sulfanylcarbonyl)pyridin-1-ium-3-carbonyl]-L-cysteine pyridin-1-ium-3,5-dicarbothioate-mononucleotide-lyase (ATP-consuming)
Reaction(IUBMB)
(1) [LarE]-L-cysteine + pyridin-1-ium-3,5-dicarboxylate mononucleotide + ATP = [LarE]-dehydroalanine + pyridin-1-ium-3-carboxylate-5-thiocarboxylate mononucleotide + AMP + diphosphate (overall reaction) [RN:
R12062 ];
(1a) ATP + pyridin-1-ium-3,5-dicarboxylate mononucleotide = diphosphate + 5-carboxy-1-(5-O-phospho-beta-D-ribofuranosyl)pyridin-1-ium-3-carbonyl adenylate [RN:
R12059 ];
(1b) 5-carboxy-1-(5-O-phospho-beta-D-ribofuranosyl)pyridin-1-ium-3-carbonyl adenylate + [LarE]-L-cysteine = AMP + [LarE]-S-[5-carboxy-1-(5-O-phosphono-beta-D-ribofuranosyl)pyridin-1-ium-3-carbonyl]-L-cysteine [RN:
R12060 ];
(1c) [LarE]-S-[5-carboxy-1-(5-O-phosphono-beta-D-ribofuranosyl)pyridin-1-ium-3-carbonyl]-L-cysteine = [LarE]-dehydroalanine + pyridin-1-ium-3-carboxylate-5-thiocarboxylate mononucleotide [RN:
R12061 ];
(2) [LarE]-L-cysteine + pyridin-1-ium-3-carboxylate-5-thiocarboxylate mononucleotide + ATP = [LarE]-dehydroalanine + pyridin-1-ium-3,5-bisthiocarboxylate mononucleotide + AMP + diphosphate (overall reaction) [RN:
R12066 ];
(2a) ATP + pyridin-1-ium-3-carboxylate-5-thiocarboxylate mononucleotide = diphosphate + 1-(5-O-phospho-beta-D-ribofuranosyl)-5-(sulfanylcarbonyl)pyridin-1-ium-3-carbonyl adenylate [RN:
R12063 ];
(2b) 1-(5-O-phospho-beta-D-ribofuranosyl)-5-(sulfanylcarbonyl)pyridin-1-ium-3-carbonyl adenylate + [LarE]-L-cysteine = AMP + [LarE]-S-[1-(5-O-phosphono-beta-D-ribofuranosyl)-5-(sulfanylcarbonyl)pyridin-1-ium-3-carbonyl]-L-cysteine [RN:
R12064 ];
(2c) [LarE]-S-[1-(5-O-phosphono-beta-D-ribofuranosyl)-5-(sulfanylcarbonyl)pyridin-1-ium-3-carbonyl]-L-cysteine = [LarE]-dehydroalanine + pyridin-1-ium-3,5-bisthiocarboxylate mononucleotide [RN:
R12065 ]
Reaction(KEGG)
Substrate
[LarE]-L-cysteine;
pyridin-1-ium-3,5-dicarboxylate mononucleotide [CPD:
C21851 ];
ATP [CPD:
C00002 ];
5-carboxy-1-(5-O-phospho-beta-D-ribofuranosyl)pyridin-1-ium-3-carbonyl adenylate [CPD:
C21877 ];
[LarE]-S-[5-carboxy-1-(5-O-phosphono-beta-D-ribofuranosyl)pyridin-1-ium-3-carbonyl]-L-cysteine;
pyridin-1-ium-3-carboxylate-5-thiocarboxylate mononucleotide [CPD:
C21878 ];
1-(5-O-phospho-beta-D-ribofuranosyl)-5-(sulfanylcarbonyl)pyridin-1-ium-3-carbonyl adenylate [CPD:
C21879 ];
[LarE]-S-[1-(5-O-phosphono-beta-D-ribofuranosyl)-5-(sulfanylcarbonyl)pyridin-1-ium-3-carbonyl]-L-cysteine
Product
[LarE]-dehydroalanine;
pyridin-1-ium-3-carboxylate-5-thiocarboxylate mononucleotide [CPD:
C21878 ];
AMP [CPD:
C00020 ];
diphosphate [CPD:
C00013 ];
5-carboxy-1-(5-O-phospho-beta-D-ribofuranosyl)pyridin-1-ium-3-carbonyl adenylate [CPD:
C21877 ];
[LarE]-S-[5-carboxy-1-(5-O-phosphono-beta-D-ribofuranosyl)pyridin-1-ium-3-carbonyl]-L-cysteine;
pyridin-1-ium-3,5-bisthiocarboxylate mononucleotide [CPD:
C21767 ];
1-(5-O-phospho-beta-D-ribofuranosyl)-5-(sulfanylcarbonyl)pyridin-1-ium-3-carbonyl adenylate [CPD:
C21879 ];
[LarE]-S-[1-(5-O-phosphono-beta-D-ribofuranosyl)-5-(sulfanylcarbonyl)pyridin-1-ium-3-carbonyl]-L-cysteine
Comment
This enzyme, found in Lactobacillus plantarum, is involved in the biosynthesis of a nickel-pincer cofactor. The process starts when one enzyme molecule adenylates pyridinium-3,5-dicarboxylate mononucleotide (P2CMN) and covalently binds the adenylated product to an intrinsic cysteine residue. Next, the enzyme cleaves the carbon-sulfur bond, liberating pyridinium-3-carboxylate-5-thiocarboxylate mononucleotide (PCTMN) and leaving a 2-aminoprop-2-enoate (dehydroalanine) residue attached to the protein. Since the cysteine residue is not regenerated in vivo, the enzyme is inactivated during the process. A second enzyme molecule then repeats the process with PCTMN, adenylating it and covalently binding it to the same cysteine residue, followed by liberation of pyridinium-3,5-bisthiocarboxylate mononucleotide (P2TMN) and the inactivation of the second enzyme molecule.
History
EC 4.4.1.37 created 2018
Orthology
K06864 pyridinium-3,5-biscarboxylic acid mononucleotide sulfurtransferase
Genes
CATE : C2869_06445 C2869_22210
THIP : N838_07935(larE) N838_08690
BUM : AXG89_23665 AXG89_29025
SINL : DSM14862_03981(larE)
GEF : FO488_13660(larE) FO488_17545(larE)
GBN : GEOBRER4_03440 GEOBRER4_19830
DMS : E8L03_07255(larE) E8L03_15165
BWH : A9C19_14220 A9C19_14270
OON : NP440_05840(larE) NP440_16065(larE)
MSEM : GMB29_06950(larE) GMB29_07365(larE)
BLEN : NCTC4824_00691 NCTC4824_02468
BCOP : JD108_16175(larE) JD108_19125(larE)
BAYD : BSPP4475_14725(larE)
LNG : BSQ50_05850 BSQ50_10040
LHW : BSQ49_00460 BSQ49_08370
LGM : LG542_05655(larE) LG542_08120(larE)
EGV : EGCR1_11140(larE) EGCR1_11185 EGCR1_12085(larE)
CBJ : H04402_00095 H04402_01251
CBEI : LF65_00621 LF65_03283
CLS : CXIVA_14630 CXIVA_19610
CSR : Cspa_c14240 Cspa_c30300
CPAS : Clopa_0770 Clopa_4087
CPAT : CLPA_c16040 CLPA_c32990
CPAE : CPAST_c16040 CPAST_c32990
CAH : CAETHG_0752(larE) CAETHG_2397(larE)
CLD : CLSPO_c01300 CLSPO_c11830
CACE : CACET_c05410 CACET_c13920
CFM : BJL90_08420 BJL90_12415
CDY : F3K33_03240(larE) F3K33_11350(larE)
GFE : Gferi_16415 Gferi_18010
CAPR : EQM14_02360(larE) EQM14_12585(larE)
PETR : QKW49_13200(larE) QKW49_17725(larE)
BPRO : PMF13cell1_04356(nadE_2)
CSCI : HDCHBGLK_00381(nadE_1) HDCHBGLK_02444(nadE_2)
ANR : Ana3638_10440(larE) Ana3638_13555(larE)
TEB : T8CH_0459 T8CH_1850 T8CH_P0032
AACX : DEACI_2248 DEACI_2545
AWI : CHL1_002283(larE) CHL1_002400(larE)
AMIC : Ami3637_07355(larE)
ABUT : Ami103574_00920(larE)
TTO : Thethe_00991 Thethe_01835
CHD : Calhy_1115 Calhy_1524
CKI : Calkr_1184 Calkr_1649
CKN : Calkro_1088 Calkro_1497
CCHA : ELD05_07750(larE) ELD05_08065(larE)
CDIA : CaldiYA01_08960 CaldiYA01_13060
MTHO : MOTHE_c25970(guaA2)
MTHZ : MOTHA_c26680(guaA2)
NCD : ACONDI_00114 ACONDI_02385
MANA : MAMMFC1_03248 MAMMFC1_04188
SLE : sle_12210(sle_12210)
RAIN : Rai3103_10330(larE)
BROO : brsh051_03180(larE)
SYY : SYNGTS_1329(slr1717)
SYT : SYNGTI_1329(slr1717)
SYS : SYNPCCN_1328(slr1717)
SYQ : SYNPCCP_1328(slr1717)
NSPH : BDGGKGIB_02456(larE)
PBOR : BSF38_03270(nadE_1)
MCAD : Pan265_06830(nadE_1)
TMM : Tmari_0968 Tmari_1079
TMI : THEMA_08980 THEMA_09515
THQ : T2812B_08615 T2812B_09090
THR : TRQ7_08930 TRQ7_09465
ALAM : RT761_00970 RT761_02574(nadE_3)
MMAK : MMKA1_14140 MMKA1_14310 MMKA1_14480 MMKA1_14650
MEYE : TL18_02430 TL18_06600
AFG : AFULGI_00005690 AFULGI_00018090
MBAK : MSBR3_0835 MSBR3_2119
MVC : MSVAZ_0321 MSVAZ_1405
MEK : MSKOL_0305 MSKOL_1347
MMET : MCMEM_1198 MCMEM_1915
MCHK : MchiMG62_15240 MchiMG62_18020
MANQ : L1994_00685(larE) L1994_02170(larE)
MFO : Metfor_0805 Metfor_2454
HALA : Hrd1104_10865(larE)
HARC : HARCEL1_11040(larE)
HALQ : Hrr1229_007315(larE)
HACB : Hbl1158_00360(larE)
MEAR : Mpt1_c07910(guaAB1)
LOKI : Lokiarch_00690(tilS)
» show all
Taxonomy
Reference
Authors
Desguin B, Goffin P, Viaene E, Kleerebezem M, Martin-Diaconescu V, Maroney MJ, Declercq JP, Soumillion P, Hols P
Title
Lactate racemase is a nickel-dependent enzyme activated by a widespread maturation system.
Journal
Sequence
Reference
Authors
Desguin B, Soumillion P, Hols P, Hausinger RP
Title
Nickel-pincer cofactor biosynthesis involves LarB-catalyzed pyridinium carboxylation and LarE-dependent sacrificial sulfur insertion.
Journal
Sequence
Reference
Authors
Fellner M, Desguin B, Hausinger RP, Hu J
Title
Structural insights into the catalytic mechanism of a sacrificial sulfur insertase of the N-type ATP pyrophosphatase family, LarE.
Journal
Sequence
Other DBs
ExplorEnz - The Enzyme Database: 4.4.1.37
ExPASy - ENZYME nomenclature database: 4.4.1.37