6.3.1.13: L-cysteine:1D-myo-inositol 2-amino-2-deoxy-alpha-D-glucopyranoside ligase
This is an abbreviated version!
For detailed information about L-cysteine:1D-myo-inositol 2-amino-2-deoxy-alpha-D-glucopyranoside ligase, go to the full flat file.
Word Map on EC 6.3.1.13
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6.3.1.13
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gsh
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oxygenase-1
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2-related
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nadph:quinone
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gamma-glutamate
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nrf2-are
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kelch-like
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nf-e2-related
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ech-associated
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oxidoreductase-1
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accys-glcn-ins
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erythroid-2-related
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drug development
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hemeoxygenase-1
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pharmacology
- 6.3.1.13
- gsh
- oxygenase-1
-
2-related
-
nadph:quinone
-
gamma-glutamate
-
nrf2-are
-
kelch-like
-
nf-e2-related
-
ech-associated
-
oxidoreductase-1
- accys-glcn-ins
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erythroid-2-related
- drug development
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hemeoxygenase-1
- pharmacology
Reaction
Synonyms
Cys:GlcN-Ins ligase, cysS2, cysteine ligase, L-cysteine:1-D-myo-inosityl 2-amino-2-deoxy-alpha-D-glucopyranoside ligase, More, MSH ligase, MshC, MshC ligase, MTCY261.29c, mycothiol cysteine ligase, mycothiol ligase, Rv2130c
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General Information
General Information on EC 6.3.1.13 - L-cysteine:1D-myo-inositol 2-amino-2-deoxy-alpha-D-glucopyranoside ligase
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malfunction
metabolism
physiological function
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mutants defective in mycothiol biosynthesis show mutations in genes coding for the glycosyltransferase (mshA) or the cysteine ligase (mshC). These mutants show low-level resistance to isoniazid but are highly resistant to ethionamide, mutations in mycothiol biosynthesis genes may contribute to isoniazid or ethionamide resistance across mycobacterial species
malfunction
Mycobacterium smegmatis mutants disrupted in mscR, coding for a dual function S-nitrosomycothiol reductase and formaldehyde dehydrogenase, and mshC, coding for a mycothiol ligase, EC 6.3.1.13, and lacking mycothiol (MSH), are more susceptible to S-nitrosoglutathione (GSNO) and aldehydes than wild-type. MSH is a cofactor for MscR, and both mshC and mscR are induced by GSNO and aldehydes. The transposon mutant, S24, disrupted in mshC, is most sensitive to killing by GSNO
malfunction
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Mycobacterium smegmatis mutants disrupted in mscR, coding for a dual function S-nitrosomycothiol reductase and formaldehyde dehydrogenase, and mshC, coding for a mycothiol ligase, EC 6.3.1.13, and lacking mycothiol (MSH), are more susceptible to S-nitrosoglutathione (GSNO) and aldehydes than wild-type. MSH is a cofactor for MscR, and both mshC and mscR are induced by GSNO and aldehydes. The transposon mutant, S24, disrupted in mshC, is most sensitive to killing by GSNO
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mycothiol cysteine ligase (MshC) is a key enzyme in the mycothiol (MSH) biosynthesis, mycothiol biosynthesis and metabolic pathway, overview
metabolism
the enzyme catalyzes the fourth step of a five step mycothiol, MSH, biosynthetic pathway
metabolism
Mycobacterium tuberculosis ATCC 25618 / H37Rv
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mycothiol cysteine ligase (MshC) is a key enzyme in the mycothiol (MSH) biosynthesis, mycothiol biosynthesis and metabolic pathway, overview
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metabolism
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the enzyme catalyzes the fourth step of a five step mycothiol, MSH, biosynthetic pathway
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mycothiol and S-nitrosomycothiol reductase are required for normal biofilm formation in Mycobacterium smegmatis
physiological function
mycothiol cysteine ligase (MshC) is a key enzyme in the mycothiol (MSH) biosynthesis. The function of MshC is irreplaceable
physiological function
Mycobacterium tuberculosis ATCC 25618 / H37Rv
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mycothiol cysteine ligase (MshC) is a key enzyme in the mycothiol (MSH) biosynthesis. The function of MshC is irreplaceable
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physiological function
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mycothiol and S-nitrosomycothiol reductase are required for normal biofilm formation in Mycobacterium smegmatis
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