From Wikipedia, the free encyclopedia
mycothiol-dependent formaldehyde dehydrogenase
Identifiers
EC no. 1.1.1.306
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / QuickGO
Search
PMC articles
PubMed articles
NCBI proteins

In enzymology, a mycothiol-dependent formaldehyde dehydrogenase ( EC 1.1.1.306) is an enzyme that catalyzes the chemical reaction

formaldehyde + mycothiol + NAD+ S-formylmycothiol + NADH + 2 H+

The 3 substrates of this enzyme are formaldehyde, mycothiol, and NAD+, whereas its 3 products are S-formylmycothiol, NADH, and H+. [1] [2] [3] [4] This enzyme catalyses the following chemical reaction

This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is formaldehyde:NAD+ oxidoreductase (mycothiol-formylating). This enzyme is also called NAD/factor-dependent formaldehyde dehydrogenase or S-(hydroxymethyl)mycothiol dehydrogenase.

References

  1. ^ Misset-Smits M, van Ophem PW, Sakuda S, Duine JA (June 1997). "Mycothiol, 1-O-(2'-[N-acetyl-L-cysteinyl]amido-2'-deoxy-alpha-D-glucopyranosyl)-D- myo-inositol, is the factor of NAD/factor-dependent formaldehyde dehydrogenase". FEBS Letters. 409 (2): 221–2. doi: 10.1016/S0014-5793(97)00510-3. PMID  9202149.
  2. ^ Norin A, Van Ophem PW, Piersma SR, Persson B, Duine JA, Jörnvall H (September 1997). "Mycothiol-dependent formaldehyde dehydrogenase, a prokaryotic medium-chain dehydrogenase/reductase, phylogenetically links different eukaroytic alcohol dehydrogenases--primary structure, conformational modelling and functional correlations". European Journal of Biochemistry. 248 (2): 282–9. doi: 10.1111/j.1432-1033.1997.00282.x. PMID  9346279.
  3. ^ Vogt RN, Steenkamp DJ, Zheng R, Blanchard JS (September 2003). "The metabolism of nitrosothiols in the Mycobacteria: identification and characterization of S-nitrosomycothiol reductase". The Biochemical Journal. 374 (Pt 3): 657–66. doi: 10.1042/BJ20030642. PMC  1223637. PMID  12809551.
  4. ^ Rawat M, Av-Gay Y (April 2007). "Mycothiol-dependent proteins in actinomycetes". FEMS Microbiology Reviews. 31 (3): 278–92. doi: 10.1111/j.1574-6976.2006.00062.x. PMID  17286835.


From Wikipedia, the free encyclopedia
mycothiol-dependent formaldehyde dehydrogenase
Identifiers
EC no. 1.1.1.306
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / QuickGO
Search
PMC articles
PubMed articles
NCBI proteins

In enzymology, a mycothiol-dependent formaldehyde dehydrogenase ( EC 1.1.1.306) is an enzyme that catalyzes the chemical reaction

formaldehyde + mycothiol + NAD+ S-formylmycothiol + NADH + 2 H+

The 3 substrates of this enzyme are formaldehyde, mycothiol, and NAD+, whereas its 3 products are S-formylmycothiol, NADH, and H+. [1] [2] [3] [4] This enzyme catalyses the following chemical reaction

This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is formaldehyde:NAD+ oxidoreductase (mycothiol-formylating). This enzyme is also called NAD/factor-dependent formaldehyde dehydrogenase or S-(hydroxymethyl)mycothiol dehydrogenase.

References

  1. ^ Misset-Smits M, van Ophem PW, Sakuda S, Duine JA (June 1997). "Mycothiol, 1-O-(2'-[N-acetyl-L-cysteinyl]amido-2'-deoxy-alpha-D-glucopyranosyl)-D- myo-inositol, is the factor of NAD/factor-dependent formaldehyde dehydrogenase". FEBS Letters. 409 (2): 221–2. doi: 10.1016/S0014-5793(97)00510-3. PMID  9202149.
  2. ^ Norin A, Van Ophem PW, Piersma SR, Persson B, Duine JA, Jörnvall H (September 1997). "Mycothiol-dependent formaldehyde dehydrogenase, a prokaryotic medium-chain dehydrogenase/reductase, phylogenetically links different eukaroytic alcohol dehydrogenases--primary structure, conformational modelling and functional correlations". European Journal of Biochemistry. 248 (2): 282–9. doi: 10.1111/j.1432-1033.1997.00282.x. PMID  9346279.
  3. ^ Vogt RN, Steenkamp DJ, Zheng R, Blanchard JS (September 2003). "The metabolism of nitrosothiols in the Mycobacteria: identification and characterization of S-nitrosomycothiol reductase". The Biochemical Journal. 374 (Pt 3): 657–66. doi: 10.1042/BJ20030642. PMC  1223637. PMID  12809551.
  4. ^ Rawat M, Av-Gay Y (April 2007). "Mycothiol-dependent proteins in actinomycetes". FEMS Microbiology Reviews. 31 (3): 278–92. doi: 10.1111/j.1574-6976.2006.00062.x. PMID  17286835.



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