| Entry |
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| Name |
glutathionylspermidine synthase;
glutathione:spermidine ligase (ADP-forming)
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| Class |
Ligases;
Forming carbon-nitrogen bonds;
Acid-D-ammonia (or amine) ligases (amide synthases)
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| Sysname |
gamma-L-glutamyl-L-cysteinyl-glycine:spermidine ligase (ADP-forming) [spermidine is numbered so that atom N-1 is in the amino group of the aminopropyl part of the molecule]
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| Reaction(IUBMB) |
glutathione + spermidine + ATP = glutathionylspermidine + ADP + phosphate [RN: R01917]
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| Reaction(KEGG) |
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| Substrate |
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| Product |
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| Comment |
Requires magnesium ions. Involved in the synthesis of trypanothione in trypanosomatids. The enzyme from Escherichia coli is bifunctional and also catalyses the glutathionylspermidine amidase (EC 3.5.1.78) reaction, resulting in a net hydrolysis of ATP.
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| Pathway |
| Glutathione metabolism | | Metabolic pathways |
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| Orthology |
| glutathionylspermidine amidase/synthetase | | glutathionylspermidine synthase |
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| Genes |
ECO: | | ECJ: | | ECD: | | EBW: | | ECOK: | | ECE: | | ECS: | | ECF: | | ETW: | | ELX: | | EOJ: | | EOI: | | EOH: | | ECG: | | EOK: | | ELR: | | ECC: | | ECP: | | ECI: | | ECV: | | ECX: | | ECW: | | ECM: | | ECY: | | ECR: | | ECQ: | | ECK: | | ECT: | | EOC: | | EUM: | | ECZ: | | ELO: | | ELN: | | ELH: | | ESE: | | ESO: | | ESM: | | ESL: | | ECL: | | EBR: | | EBD: | | EKO: | | EKF: | | EAB: | | EDH: | | EDJ: | | EIH: | | ENA: | | ELU: | | EUN: | | ELW: | | ELL: | | ELC: | | ELD: | | ELP: | | EBL: | | EBE: | | ELF: | | ECOA: | | EFE: | | EBT: | | STY: | | STT: | | SEX: | | STM: | | SEO: | | SEV: | | SEY: | | SEM: | | SEJ: | | SEB: | | SEF: | | SETU: | | SPT: | | SEK: | | SPQ: | | SEI: | | SEC: | | SEH: | | SHB: | | SEE: | | SEW: | | SEA: | | SED: | | SEL: | | SET: | | SENJ: | | SES: | | SBG: | | SFL: | | SFX: | | SFV: | | SFE: | | SSN: | | SSJ: | | SBO: | | SBC: | | SDY: | | ENT: | | ENC: | | ENO: | | ECLO: | | ESC: | | EEC: | | ENL: | | EAS: | | EAE: | | EAR: | | KPN: | | KPU: | | KPM: | | KPP: | | KPE: | | KPO: | | KVA: | | KOX: | | CKO: | | CRO: | | PMR: | | EIC: | | ETR: | | ETD: | | ETC: | | MMK: | | ROR: | | EBF: | | HIU: | | HPR: | | MSU: | | ASU: | | AAP: | | AAT: | | AAO: | | AAN: | | MCT: | | PHA: | | GNI: | | GPS: | | PIN: | | MMW: | | SAGA: | | REH: | | CTI: | | HPY: | | HPJ: | | HPA: | | HPS: | | HPG: | | HPP: | | HPB: | | HPL: | | HPC: | | HPM: | | HHE: | | HAC: | | HMS: | | HFE: | | WSU: | | TDN: | | SKU: | | CJE: | | CJJ: | | CJU: | | CJN: | | CJR: | | CJD: | | CFF: | | CCV: | | CCO: | | CLA: | | ABU: | | ANT: | | SDL: | | NSA: | | SUN: | | GLO: | | BRA: | | BBT: | | AEX: | | NAR: | | RRF: | | RCE: | | AZL: | | BAN: | | BAR: | | BAT: | | BAH: | | BAI: | | BAL: | | BCE: | | BCA: | | BCZ: | | BCR: | | BCB: | | BCU: | | BCG: | | BCQ: | | BCX: | | BCY: | | BTK: | | BTL: | | BTB: | | BWE: | | BPF: | | BMQ: | | BMD: | | GWC: | | ESI: | | EAT: | | BBE: | | PJD: | | GYM: | | HMO: | | VPR: | | TCU: | | SUS: | | HHY: | | DFE: | | SLI: | | RSI: | | CYN: | | AVA: | | TER: | |
» show all
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| Reference |
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| Authors |
Smith K, Nadeau K, Bradley M, Walsh C, Fairlamb AH. |
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| Title |
Purification of glutathionylspermidine and trypanothione synthetases from Crithidia fasciculata. |
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| Journal |
Protein. Sci. 1 (1992) 874-83. |
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| Organism |
Crithidia fasciculata |
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| Reference |
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| Authors |
Bollinger JM Jr, Kwon DS, Huisman GW, Kolter R, Walsh CT. |
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| Title |
Glutathionylspermidine metabolism in Escherichia coli. Purification, cloning, overproduction, and characterization of a bifunctional glutathionylspermidine synthetase/amidase. |
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| Journal |
J. Biol. Chem. 270 (1995) 14031-41. |
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| Organism |
Escherichia coli [GN: eco] |
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| Sequence |
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| Other DBs |
ExplorEnz - The Enzyme Database: IUBMB Enzyme Nomenclature: ExPASy - ENZYME nomenclature database: BRENDA, the Enzyme Database: CAS: 9077-09-2 |
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