| Entry |
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| Name |
L-cysteine:1D-myo-inositol 2-amino-2-deoxy-alpha-D-glucopyranoside ligase;
MshC;
MshC ligase;
Cys:GlcN-Ins ligase;
mycothiol ligase
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| Class |
Ligases;
Forming carbon-nitrogen bonds;
Acid-D-ammonia (or amine) ligases (amide synthases)
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| Sysname |
L-cysteine:1-O-(2-amino-2-deoxy-alpha-D-glucopyranosyl)-1D-myo-inositol ligase (AMP-forming)
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| Reaction(IUBMB) |
1-O-(2-amino-2-deoxy-alpha-D-glucopyranosyl)-1D-myo-inositol + L-cysteine + ATP = 1-O-[2-(L-cysteinamido)-2-deoxy-alpha-D-glucopyranosyl]-1D-myo-inositol + AMP + diphosphate [RN: R09591]
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| Reaction(KEGG) |
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| Substrate |
1-O-(2-amino-2-deoxy-alpha-D-glucopyranosyl)-1D-myo-inositol [CPD: C19702];
L-cysteine [CPD: C00097];
ATP [CPD: C00002]
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| Product |
1-O-[2-(L-cysteinamido)-2-deoxy-alpha-D-glucopyranosyl]-1D-myo-inositol [CPD: C19703];
AMP [CPD: C00020];
diphosphate [CPD: C00013]
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| Comment |
This enzyme is a key enzyme in the biosynthesis of mycothiol, a small molecular weight thiol found in Mycobacteria spp. and other actinomycetes. Mycothiol plays a fundamental role in these organisms by helping to provide protection from the effects of reactive oxygen species and electrophiles, including many antibiotics. The enzyme may represent a novel target for new classes of antituberculars [2].
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| Orthology |
| L-cysteine:1D-myo-inositol 2-amino-2-deoxy-alpha-D-glucopyranoside ligase |
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| Genes |
MTU: | | MTV: | | MTC: | | MRA: | | MTF: | | MTB: | | MTK: | | MTZ: | | MTG: | | MTI: | | MTE: | | MTL: | | MTO: | | MTD: | | MTN: | | MTJ: | | MTUB: | | MBO: | | MBB: | | MBT: | | MBM: | | MBK: | | MAF: | | MCE: | | MCQ: | | MCV: | | MCX: | | MCZ: | | MLE: | | MLB: | | MPA: | | MAV: | | MIT: | | MIR: | | MIA: | | MID: | | MSM: | | MSG: | | MSA: | | MUL: | | MVA: | | MGI: | | MSP: | | MAB: | | MMV: | | MMC: | | MKM: | | MJL: | | MJD: | | MMI: | | MRH: | | MMM: | | MCB: | | MLI: | | ASD: | | CGL: | | CGB: | | CGU: | | CGT: | | CEF: | | CDI: | | CDP: | | CDH: | | CDT: | | CDE: | | CDR: | | CDA: | | CDZ: | | CDB: | | CDS: | | CDD: | | CDW: | | CDV: | | CJK: | | CUR: | | CUA: | | CAR: | | CKP: | | CPU: | | CPL: | | CPG: | | CPP: | | CPK: | | CPQ: | | CPX: | | CPZ: | | COR: | | COP: | | COD: | | COS: | | COI: | | COU: | | CRD: | | CUL: | | CUC: | | CUE: | | CVA: | | CHN: | | CCN: | | NFA: | | NCY: | | NBR: | | RHA: | | RER: | | ROP: | | REQ: | | GBR: | | GPO: | | GOR: | | TPR: | | SRT: | | SCO: | | SMA: | | SGR: | | SCB: | | SSX: | | SVL: | | SCT: | | SCY: | | SFA: | | SBH: | | SHY: | | SHO: | | SVE: | | SDV: | | SALB: | | STRP: | | KSK: | | CMI: | | CMS: | | CMC: | | ART: | | AAU: | | ACH: | | AAI: | | APN: | | ARR: | | RSA: | | KRH: | | MLU: | | RMU: | | RDN: | | BCV: | | BFA: | | JDE: | | KSE: | | XCE: | | IVA: | | SKE: | | CFL: | | CFI: | | CGA: | | ICA: | | PFR: | | PPC: | | MPH: | | NCA: | | KFL: | | TFU: | | NDA: | | NAL: | | TCU: | | SRO: | | FRA: | | FRE: | | FRI: | | FAL: | | FSY: | | ACE: | | NML: | | GOB: | | BSD: | | MMAR: | | KRA: | | SEN: | | SVI: | | TBI: | | AMD: | | AMN: | | AMM: | | PDX: | | AMI: | | SESP: | | STP: | | SAQ: | | MAU: | | MIL: | | VMA: | | AMS: | | ASE: | | CAI: | | SNA: | | AFO: | | AYM: | | RRS: | | RCA: | | CAU: | | CAG: | | CHL: | | HAU: | | TRO: | | STI: | | TTR: | |
» show all
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| Reference |
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| Authors |
Fan F, Luxenburger A, Painter GF, Blanchard JS |
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| Title |
Steady-state and pre-steady-state kinetic analysis of Mycobacterium smegmatis cysteine ligase (MshC). |
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| Journal |
Biochemistry. 46 (2007) 11421-9. |
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| Organism |
Mycobacterium smegmatis [GN: msm] |
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| Reference |
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| Authors |
Gutierrez-Lugo MT, Newton GL, Fahey RC, Bewley CA |
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| Title |
Cloning, expression and rapid purification of active recombinant mycothiol ligase as B1 immunoglobulin binding domain of streptococcal protein G, glutathione-S-transferase and maltose binding protein fusion proteins in Mycobacterium smegmatis. |
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| Journal |
Protein. Expr. Purif. 50 (2006) 128-36. |
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| Organism |
Mycobacterium smegmatis [GN: msm] |
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| Reference |
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| Authors |
Tremblay LW, Fan F, Vetting MW, Blanchard JS |
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| Title |
The 1.6 A crystal structure of Mycobacterium smegmatis MshC: the penultimate enzyme in the mycothiol biosynthetic pathway. |
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| Journal |
Biochemistry. 47 (2008) 13326-35. |
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| Organism |
Mycobacterium smegmatis [GN: msm] |
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| Other DBs |
ExplorEnz - The Enzyme Database: IUBMB Enzyme Nomenclature: ExPASy - ENZYME nomenclature database: BRENDA, the Enzyme Database: |
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