KEGG   ENZYME: 6.3.1.13Help
Entry
EC 6.3.1.13                 Enzyme                                 

Name
L-cysteine:1D-myo-inositol 2-amino-2-deoxy-alpha-D-glucopyranoside ligase;
MshC;
MshC ligase;
Cys:GlcN-Ins ligase;
mycothiol ligase
Class
Ligases;
Forming carbon-nitrogen bonds;
Acid-D-ammonia (or amine) ligases (amide synthases)
BRITE hierarchy
Sysname
L-cysteine:1-O-(2-amino-2-deoxy-alpha-D-glucopyranosyl)-1D-myo-inositol ligase (AMP-forming)
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]
Reaction(KEGG)
Substrate
1-O-(2-amino-2-deoxy-alpha-D-glucopyranosyl)-1D-myo-inositol [CPD:C19702];
L-cysteine [CPD:C00097];
ATP [CPD:C00002]
Product
1-O-[2-(L-cysteinamido)-2-deoxy-alpha-D-glucopyranosyl]-1D-myo-inositol [CPD:C19703];
AMP [CPD:C00020];
diphosphate [CPD:C00013]
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].
History
EC 6.3.1.13 created 2009
Orthology
K15526  
L-cysteine:1D-myo-inositol 2-amino-2-deoxy-alpha-D-glucopyranoside ligase
Genes
MTU: 
Rv2130c(mshC)
MTV: 
MTC: 
MT2188(cysS)
MRA: 
MRA_2144(cysS1)
MTF: 
MTB: 
MTK: 
MTZ: 
MTG: 
MTI: 
MTE: 
MTUR: 
CFBS_2257(cysS1)
MTL: 
MTO: 
MTD: 
UDA_2130c(cysS2)
MTN: 
MTJ: 
MTUB: 
MTUC: 
MTUE: 
MTX: 
MTUL: 
MTUT: 
HKBT1_2248(cysS1)
MTUU: 
HKBT2_2250(cysS1)
MTQ: 
HKBS1_2254(cysS1)
MBO: 
Mb2154c(cysS)
MBB: 
BCG_2147c(cysS2)
MBT: 
JTY_2141(cysS2)
MBM: 
MBK: 
MAF: 
MAF_21420(cysS2)
MCE: 
MCAN_21541(cysS2)
MCQ: 
MCV: 
MCX: 
MCZ: 
MLE: 
ML1302(cysS)
MLB: 
MLBr_01302(cysS2)
MPA: 
MAP1876c(cysS)
MAO: 
MAV: 
MAV_2361(cysS)
MIT: 
MIR: 
MIA: 
MID: 
MYO: 
MSM: 
MSG: 
MSMEI_4091(cysS2)
MSA: 
MUL: 
MUL_2360(mshC)
MVA: 
MGI: 
MSP: 
MAB: 
MABB: 
MMV: 
MMC: 
MKM: 
MJL: 
MJD: 
MMI: 
MMAR_3110(mshC)
MRH: 
MMM: 
MCB: 
MLI: 
MKN: 
MNE: 
ASD: 
AS9A_1960(mshC)
CGL: 
NCgl1457(cysS)
CGB: 
cg1709(cysS)
CGU: 
WA5_1457(CysS)
CGT: 
CGS: 
CGG: 
CGM: 
cgp_1709(mshC)
CEF: 
CE1639(cysS)
CDI: 
DIP1261(cysS)
CDP: 
CD241_1191(cysS2)
CDH: 
CDT: 
CDE: 
CDR: 
CDA: 
CDZ: 
CD31A_1272(cysS2)
CDB: 
CDBH8_1239(cysS2)
CDS: 
CDC7B_1255(cysS2)
CDD: 
CDW: 
CDPW8_1240(cysS2)
CDV: 
CJK: 
jk0368(cysS2) jk0956(cysS1)
CUR: 
CUA: 
CAR: 
CKP: 
CPU: 
CPL: 
CPG: 
CPP: 
CPK: 
CPQ: 
CPX: 
CPZ: 
COR: 
COP: 
Cp31_1058(mshC)
COD: 
COS: 
COI: 
COU: 
CRD: 
CRES_1038(mshC)
CUL: 
CUC: 
CUE: 
CVA: 
CVAR_1445(mshC)
CHN: 
CCN: 
CTER: 
CMD: 
CAZ: 
CFN: 
CCG: 
CVT: 
CGY: 
CGLY_08655(mshC2)
CAX: 
NFA: 
nfa29340(cysS)
NCY: 
NBR: 
NNO: 
RHA: 
RER: 
RER_31960(mshC)
REY: 
ROP: 
ROP_06130(mshC)
ROA: 
REQ: 
REQ_22990(mshC)
RPY: 
GBR: 
GPO: 
GOR: 
TPR: 
SRT: 
SCO: 
SCO1663(cysS)
SMA: 
SAV_6647(cysS)
SGR: 
SGR_5840(cysS2)
SCB: 
SCAB_73151(cysS2)
SSX: 
SVL: 
SCT: 
SCAT_5134(cysS)
SCY: 
SFA: 
SBH: 
SBI_08453(cysS2)
SHY: 
SHO: 
SVE: 
SDV: 
SALB: 
STRP: 
F750_1464(mshC)
SFI: 
SCI: 
SRC: 
SALU: 
SLV: 
KSK: 
KSE_66390(mshC)
CMI: 
CMM_1694(cysS2)
CMS: 
CMS_1669(cysS)
CMC: 
CMN_01673(mshC)
ART: 
AAU: 
ACH: 
AAI: 
APN: 
ARR: 
RSA: 
KRH: 
KRH_13920(mshC)
MLU: 
RMU: 
RDN: 
BCV: 
BFA: 
JDE: 
KSE: 
DNI: 
XCE: 
IVA: 
SKE: 
CFL: 
CFI: 
CGA: 
ICA: 
PFR: 
PPC: 
MPH: 
MLP_17040(mshC)
NCA: 
KFL: 
TFU: 
Tfu_1832(cysS)
NDA: 
NAL: 
B005_4133(mshC)
TCU: 
SRO: 
FRA: 
FRE: 
FRI: 
FAL: 
FRAAL2858(cysS2)
FSY: 
ACE: 
NML: 
GOB: 
BSD: 
BLASA_2691(cysS2)
MMAR: 
KRA: 
SEN: 
SACE_2226(cysS2)
SVI: 
TBI: 
AMD: 
AMED_4930(cysS)
AMN: 
AMM: 
AMES_4871(cysS)
AMZ: 
B737_4871(cysS)
AOI: 
AORI_3794(cysS)
AJA: 
AMQ: 
PDX: 
AMI: 
SESP: 
BN6_31410(mshC)
KAL: 
STP: 
SAQ: 
MAU: 
MIL: 
VMA: 
AMS: 
ASE: 
ACPL_5266(mshC)
ACTN: 
L083_5113(cysS)
AFS: 
CAI: 
SNA: 
ASG: 
AFO: 
AYM: 
RRS: 
RCA: 
CAU: 
CAG: 
CHL: 
HAU: 
TRO: 
trd_1909(cysS)
STI: 
TTR: 
 » show all
Taxonomy
Reference
1  [PMID:17848100]
  Authors
Fan F, Luxenburger A, Painter GF, Blanchard JS
  Title
Steady-state and pre-steady-state kinetic analysis of Mycobacterium smegmatis cysteine ligase (MshC).
  Journal
Biochemistry. 46 (2007) 11421-9.
  Sequence
Reference
2  [PMID:16908186]
  Authors
Gutierrez-Lugo MT, Newton GL, Fahey RC, Bewley CA
  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.
  Journal
Protein. Expr. Purif. 50 (2006) 128-36.
Reference
3  [PMID:19053270]
  Authors
Tremblay LW, Fan F, Vetting MW, Blanchard JS
  Title
The 1.6 A crystal structure of Mycobacterium smegmatis MshC: the penultimate enzyme in the mycothiol biosynthetic pathway.
  Journal
Biochemistry. 47 (2008) 13326-35.
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 

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