KEGG   ENZYME: 6.2.2.3
Entry
EC 6.2.2.3                  Enzyme                                 

Name
thiazoline synthase
Class
Ligases;
Forming carbon-sulfur bonds;
Amide---thiol ligases
Sysname
[protein]-(L-amino acyl-L-cysteine) cyclodehydratase (2-thiazoline-forming)
Reaction(IUBMB)
ATP + a [protein]-(L-amino acyl-L-cysteine) = ADP + phosphate + a [protein]-(1S,4R)-2-(C-substituted-aminomethyl)-4-acyl-2-thiazoline
Substrate
ATP [CPD:C00002];
[protein]-(L-amino acyl-L-cysteine)
Product
ADP [CPD:C00008];
phosphate [CPD:C00009];
[protein]-(1S,4R)-2-(C-substituted-aminomethyl)-4-acyl-2-thiazoline
Comment
Requires Mg2+. The enzyme, which participates in the biosynthesis of some ribosomal peptide natural products (RiPPs) such as the trunkamides, converts L-cysteine residues to thiazoline rings. The enzyme requires two domains - a cyclodehydratase domain, known as a YcaO domain, and a substrate recognition domain (RRE domain) that controls the regiospecificity of the enzyme. The RRE domain can either be fused to the YcaO domain or occur as a separate protein; however both domains are required for activity. The enzyme can process multiple L-cysteine residues within the same substrate peptide, and all enzymes characterized so far follow a defined order, starting with the L-cysteine closest to the C-terminus. The reaction involves phosphorylation of the preceding ribosomal peptide backbone amide bond, forming ADP and a phosphorylated intermediate, followed by release of the phosphate group. In some cases the enzyme catalyses a side reaction in which the phosphorylated intermediate reacts with ADP to form AMP and diphosphate. This activity is also catalysed by the related enzyme EC 6.2.2.2, oxazoline synthase. That enzyme differs by having an RRE domain that also recognizes L-serine and L-threonine residues, which are converted to oxazoline and methyloxazoline rings, respectively.
History
EC 6.2.2.3 created 2020
Orthology
K24411  oxazoline/thiazoline synthase
Genes
PGB: H744_2c1844
PRR: AT705_20070
PVB: J5X90_21760
MPSY: CEK71_11635
TIG: THII_1452
AQL: BXU06_00280
BMA: BMA0023
BMV: BMASAVP1_A2869
BML: BMA10229_A2214
BMN: BMA10247_2493
BMAL: DM55_418
BMAE: DM78_499
BMAQ: DM76_398
BMAI: DM57_2183
BMAF: DM51_3009
BMAZ: BM44_807
BMAB: BM45_414
BPS: BPSL0600
BPSE: BDL_1405
BPSM: BBQ_2827
BPSD: BBX_3353
BPK: BBK_886
BPSH: DR55_494
BPSA: BBU_1551
BPSO: X996_101
BUT: X994_2115
BTE: BTH_I0517
BTQ: BTQ_539
BTJ: BTJ_1946
BTZ: BTL_3182
BTD: BTI_3187
BTV: BTHA_3465
BTHE: BTN_1530
BTHM: BTRA_60
BTHA: DR62_1717
BTHL: BG87_25
BOK: DM82_26
BOC: BG90_995
BCN: Bcen_5136
BCJ: BCAM0032
BCEO: I35_4032
BAM: Bamb_4992
BCED: DM42_5115
BSEM: WJ12_25405
BSTG: WT74_32040
BUL: BW21_3336
AAV: Aave_3061
AAA: Acav_2221
DAC: Daci_4368
SAT: SYN_00274
BJA: blr4538(blr4538)
MET: M446_3967
MNO: Mnod_4676
MSC: BN69_1551
SHUM: STHU_40390
SWO: Swol_1788
SALB: XNR_3461
SMAL: SMALA_2873
SBH: SBI_06840
SVE: SVEN_6223
SLAU: SLA_3079
MLV: CVS47_02157(ycaO)
LMOI: VV02_06540
TCU: Tcur_2767
AOI: AORI_1830
AMYY: YIM_41055
AORI: SD37_32060
ALO: CRK57519
MAR: MAE_33130
MPK: VL20_3234
CYT: cce_4099
TER: Tery_2355
FTJ: FTUN_1196
PLT: Plut_0880
 » show all
Reference
1  [PMID:20540059]
  Authors
McIntosh JA, Schmidt EW
  Title
Marine molecular machines: heterocyclization in cyanobactin biosynthesis.
  Journal
Chembiochem 11:1413-21 (2010)
DOI:10.1002/cbic.201000196
Reference
2  [PMID:20210311]
  Authors
McIntosh JA, Donia MS, Schmidt EW
  Title
Insights into heterocyclization from two highly similar enzymes.
  Journal
J Am Chem Soc 132:4089-91 (2010)
DOI:10.1021/ja9107116
Reference
3  [PMID:24214017]
  Authors
Koehnke J, Bent AF, Zollman D, Smith K, Houssen WE, Zhu X, Mann G, Lebl T, Scharff R, Shirran S, Botting CH, Jaspars M, Schwarz-Linek U, Naismith JH
  Title
The cyanobactin heterocyclase enzyme: a processive adenylase that operates with a defined order of reaction.
  Journal
Angew Chem Int Ed Engl 52:13991-6 (2013)
DOI:10.1002/anie.201306302
Reference
4  [PMID:26098679]
  Authors
Koehnke J, Mann G, Bent AF, Ludewig H, Shirran S, Botting C, Lebl T, Houssen W, Jaspars M, Naismith JH
  Title
Structural analysis of leader peptide binding enables leader-free cyanobactin processing.
  Journal
Nat Chem Biol 11:558-563 (2015)
DOI:10.1038/nchembio.1841
Reference
5  [PMID:30912640]
  Authors
Ge Y, Czekster CM, Miller OK, Botting CH, Schwarz-Linek U, Naismith JH
  Title
Insights into the Mechanism of the Cyanobactin Heterocyclase Enzyme.
  Journal
Biochemistry 58:2125-2132 (2019)
DOI:10.1021/acs.biochem.9b00084
Other DBs
ExplorEnz - The Enzyme Database: 6.2.2.3
IUBMB Enzyme Nomenclature: 6.2.2.3
ExPASy - ENZYME nomenclature database: 6.2.2.3
BRENDA, the Enzyme Database: 6.2.2.3

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