Any feedback?
No. of entries
Information on EC 2.3.1.189 - mycothiol synthase
for references in articles please use BRENDA:EC2.3.1.189
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree 2 Transferases
2.3 Acyltransferases
2.3.1 Transferring groups other than aminoacyl groups
2.3.1.189 mycothiol synthase
IUBMB Comments
This enzyme catalyses the last step in the biosynthesis of mycothiol, the major thiol in most actinomycetes, including Mycobacterium . The enzyme is a member of a large family of GCN5-related N-acetyltransferases (GNATs) . The enzyme has been purified from Mycobacterium tuberculosis H37Rv. Acetyl-CoA is the preferred CoA thioester but propionyl-CoA is also a substrate .
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
- 2.3.1.189
- tuberculosis
- actinomycetes
- n-acetyltransferase
- smegmatis
-
gnat
- amine
-
gcn5-related
-
thiol-disulfide
- accys-glcn-ins
- diagnostics
showSynonyms
rv0819, mycothiol synthase, msh synthase, more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
MSH acetyltransferase
MSH synthase
MshD
Rv0819
MshD
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
desacetylmycothiol + acetyl-CoA = CoA + mycothiol
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
MetaCyc
mycothiol biosynthesis
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:desacetylmycothiol O-acetyltransferase
This enzyme catalyses the last step in the biosynthesis of mycothiol, the major thiol in most actinomycetes, including Mycobacterium [1]. The enzyme is a member of a large family of GCN5-related N-acetyltransferases (GNATs) [2]. The enzyme has been purified from Mycobacterium tuberculosis H37Rv. Acetyl-CoA is the preferred CoA thioester but propionyl-CoA is also a substrate [3].
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
desacetylmycothiol + acetyl-CoA
mycothiol + coenzyme A
-
Substrates: last step in biosynthesis of mycothiol, the major thiol in most actinomycetes
Products: -
Products: -
?
desacetylmycothiol + acetyl-CoA
mycothiol + coenzyme A
-
Substrates: -
Products: -
Products: -
?
desacetylmycothiol + acetyl-CoA
mycothiol + coenzyme A
Substrates: last step in biosynthesis of mycothiol, the major thiol in most actinomycetes
Products: -
Products: -
?
desacetylmycothiol + acetyl-CoA
mycothiol + coenzyme A
Substrates: -
Products: -
Products: -
?
desacetylmycothiol + acetyl-CoA
mycothiol + coenzyme A
Substrates: last step in biosynthesis of mycothiol, the major thiol in most actinomycetes
Products: -
Products: -
?
desacetylmycothiol + acetyl-CoA
mycothiol + coenzyme A
Substrates: -
Products: -
Products: -
?
desacetylmycothiol + acetyl-CoA
mycothiol + coenzyme A
-
Substrates: last step in biosynthesis of mycothiol, the major thiol in most actinomycetes
Products: -
Products: -
?
desacetylmycothiol + acetyl-CoA
mycothiol + coenzyme A
-
Substrates: -
Products: -
Products: -
?
desacetylmycothiol + acetyl-CoA
mycothiol + coenzyme A
-
Substrates: last step in biosynthesis of mycothiol, the major thiol in most actinomycetes
Products: -
Products: -
?
desacetylmycothiol + acetyl-CoA
mycothiol + coenzyme A
-
Substrates: -
Products: -
Products: -
?
desacetylmycothiol + acetyl-CoA
mycothiol + coenzyme A
-
Substrates: last step in biosynthesis of mycothiol, the major thiol in most actinomycetes
Products: -
Products: -
?
desacetylmycothiol + acetyl-CoA
mycothiol + coenzyme A
-
Substrates: -
Products: -
Products: -
?
desacetylmycothiol + acetyl-CoA
mycothiol + coenzyme A
-
Substrates: last step in biosynthesis of mycothiol, the major thiol in most actinomycetes
Products: -
Products: -
?
desacetylmycothiol + acetyl-CoA
mycothiol + coenzyme A
-
Substrates: -
Products: -
Products: -
?
desacetylmycothiol + acetyl-CoA
mycothiol + coenzyme-A
Substrates: this enzyme catalyses the last step in the biosynthesis of mycothiol, the major thiol in most actinomycetes
Products: -
Products: -
?
desacetylmycothiol + acetyl-CoA
mycothiol + coenzyme-A
-
Substrates: -
Products: -
Products: -
?
desacetylmycothiol + acetyl-CoA
mycothiol + coenzyme-A
Substrates: -
Products: -
Products: -
?
desacetylmycothiol + acetyl-CoA
mycothiol + coenzyme-A
-
Substrates: -
Products: -
Products: -
?
desacetylmycothiol + acetyl-CoA
mycothiol + coenzyme-A
Substrates: this enzyme catalyses the last step in the biosynthesis of mycothiol, the major thiol in most actinomycetes
Products: -
Products: -
?
desacetylmycothiol + acetyl-CoA
mycothiol + coenzyme-A
Substrates: -
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
desacetylmycothiol + acetyl-CoA
mycothiol + coenzyme A
-
Substrates: last step in biosynthesis of mycothiol, the major thiol in most actinomycetes
Products: -
Products: -
?
desacetylmycothiol + acetyl-CoA
mycothiol + coenzyme A
Substrates: last step in biosynthesis of mycothiol, the major thiol in most actinomycetes
Products: -
Products: -
?
desacetylmycothiol + acetyl-CoA
mycothiol + coenzyme A
Substrates: last step in biosynthesis of mycothiol, the major thiol in most actinomycetes
Products: -
Products: -
?
desacetylmycothiol + acetyl-CoA
mycothiol + coenzyme A
-
Substrates: last step in biosynthesis of mycothiol, the major thiol in most actinomycetes
Products: -
Products: -
?
desacetylmycothiol + acetyl-CoA
mycothiol + coenzyme A
-
Substrates: last step in biosynthesis of mycothiol, the major thiol in most actinomycetes
Products: -
Products: -
?
desacetylmycothiol + acetyl-CoA
mycothiol + coenzyme A
-
Substrates: last step in biosynthesis of mycothiol, the major thiol in most actinomycetes
Products: -
Products: -
?
desacetylmycothiol + acetyl-CoA
mycothiol + coenzyme A
-
Substrates: last step in biosynthesis of mycothiol, the major thiol in most actinomycetes
Products: -
Products: -
?
desacetylmycothiol + acetyl-CoA
mycothiol + coenzyme-A
Substrates: this enzyme catalyses the last step in the biosynthesis of mycothiol, the major thiol in most actinomycetes
Products: -
Products: -
?
desacetylmycothiol + acetyl-CoA
mycothiol + coenzyme-A
-
Substrates: -
Products: -
Products: -
?
desacetylmycothiol + acetyl-CoA
mycothiol + coenzyme-A
Substrates: -
Products: -
Products: -
?
desacetylmycothiol + acetyl-CoA
mycothiol + coenzyme-A
Substrates: this enzyme catalyses the last step in the biosynthesis of mycothiol, the major thiol in most actinomycetes
Products: -
Products: -
?
desacetylmycothiol + acetyl-CoA
mycothiol + coenzyme-A
Substrates: -
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Infections
Mycothiol acetyltransferase (Rv0819) of Mycobacterium tuberculosis is a potential biomarker for direct diagnosis of tuberculosis using patient serum specimens.
Tuberculosis
A mycothiol synthase mutant of Mycobacterium tuberculosis has an altered thiol-disulfide content and limited tolerance to stress.
Tuberculosis
Crystal structure of mycothiol synthase (Rv0819) from Mycobacterium tuberculosis shows structural homology to the GNAT family of N-acetyltransferases.
Tuberculosis
Identification of the mycothiol synthase gene (mshD) encoding the acetyltransferase producing mycothiol in actinomycetes.
Tuberculosis
The substrate-induced conformational change of Mycobacterium tuberculosis mycothiol synthase.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
malfunction
production of a Mycobacterium smegmatis transposon mutant blocked in the production of mycothill as the result of lacking the transacetylase activity of mycothiol synthase
malfunction
-
the mycothiol synthase mutant mshD::Tn5, produces high levels of Cys-GlcN-Ins along with two novel thiols, N-formyl-Cys-GlcN-Ins and N-succinyl-Cys-GlcN-Ins, and a small amount of mycothiol. The nonenzymatic reaction of acyl-coenzyme A with Cys-GlcN-Ins to produce acyl-Cys-GlcN-Ins is a facile reaction under physiologic conditions, with succinyl-CoA being an order of magnitude more reactive than acetyl-CoA. The uncatalyzed reaction rates are adequate to account for the observed production of N-succinyl-Cys-GlcN-Ins and mycothiol under physiologic conditions. The N-acyl-Cys-GlcN-Ins compounds are maintained in a substantially reduced state in the mutant but that Cys-GlcN-Ins exists in disulfide forms at 5 to 40% at different stages of growth. Mycothiol is able to facilitate reduction of N-succinyl-Cys-GlcN-Ins disulfide through thiol-disulfide exchange, but N-formyl-Cys-GlcN-Ins is ineffective. The oxidized state of Cys-GlcN-Ins in cells appears to result from a high susceptibility to autoxidation and a low capacity of the cell to reduce its disulfide forms. The mutant exhibits no enhanced sensitivity to hydrogen peroxide, tert-butyl hydroperoxide, or cumene hydroperoxide relative to the parent strain, suggesting that the most abundant thiol, N-formyl-Cys-GlcN-Ins, functions as a substitute for mycothiol
malfunction
-
production of a Mycobacterium smegmatis transposon mutant blocked in the production of mycothill as the result of lacking the transacetylase activity of mycothiol synthase
-
Show AA Sequence and Transmembrane Helices (2495 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
vapor diffusion under oil, 1.8 A resolution structure of MshD in complex with the disulfide of CoA and desacetylmycothiol
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloned in pQE31 plasmid and transformed into Escherichia coli M15 (pREP4)
the Rv0819 gene encoding MshD (residues 1315) is amplified from Mycobacterium tuberculosis genomic DNA using PCR and cloned into the pET28a(+) plasmid. This vector construction adds six histidine residues and a thrombin cleavage sequence to the N-terminus to facilitate protein purification. Expression in Escherichia coli stain BL21(DE3)pLysS
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
diagnostics
diagnostics
the enzyme is a potential biomarker for direct diagnosis of tuberculosis using patient serum specimens
diagnostics
-
the enzyme is a potential biomarker for direct diagnosis of tuberculosis using patient serum specimens
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Newton, G.L.; Buchmeier, N.; Fahey, R.C.
Biosynthesis and functions of mycothiol, the unique protective thiol of actinobacteria
Microbiol. Mol. Biol. Rev.
72
471-494
2008
Corynebacterium glutamicum, Mycobacterium tuberculosis (P9WJM7), Mycobacterium tuberculosis H37Rv (P9WJM7), Mycolicibacterium smegmatis, Rhodococcus jostii, Rhodococcus jostii RHA-1, Streptomyces coelicolor
brenda
Koledin, T.; Newton, G.L.; Fahey, R.C.
Identification of the mycothiol synthase gene (mshD) encoding the acetyltransferase producing mycothiol in actinomycetes
Arch. Microbiol.
178
331-337
2002
Mycobacterium tuberculosis (P9WJM7), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WJM7)
brenda
Newton, G.L.
Ta, P.; Fahey, R.C.: A mycothiol synthase mutant of Mycobacterium smegmatis produces novel thiols and has an altered thiol redox status
J. Bacteriol.
187
7309-7316
2005
Mycobacterium tuberculosis
brenda
Vetting, M.W.; Yu, M.; Rendle, P.M.; Blanchard, J.S.
The substrate-induced conformational change of Mycobacterium tuberculosis mycothiol synthase
J. Biol. Chem.
281
2795-2802
2006
Mycobacterium tuberculosis (P9WJM7), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WJM7)
brenda
Vetting, M.W.; Roderick, S.L.; Yu, M.; Blanchard, J.S.
Crystal structure of mycothiol synthase (Rv0819) from Mycobacterium tuberculosis shows structural homology to the GNAT family of N-acetyltransferases
Protein Sci.
12
1954-1959
2003
Mycobacterium tuberculosis (P9WJM7), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WJM7)
brenda
Zeitoun, H.; Bahey-El-Din, M.; Kassem, M.; Aboushleib, H.
Mycothiol acetyltransferase (Rv0819) of Mycobacterium tuberculosis is a potential biomarker for direct diagnosis of tuberculosis using patient serum specimens
Lett. Appl. Microbiol.
65
504-511
2017
Mycobacterium tuberculosis (P9WJM7), Mycobacterium tuberculosis, Mycobacterium tuberculosis ATCC 25618 (P9WJM7)
brenda
EXTERNAL LINKS (specific for EC-Number 2.3.1.189)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2026.1 (March 2026)
About BRENDA
Social media
Help
Survey
Download
Contribution
Legal
Curated at
Member of
![DSMZ Digital Diversity]()
![Global Core Biodata Resource]()
![ELIXIR Core Data Resource]()
![German Network for Bioinformatics Infrastructure]()
