1.2.1.27: methylmalonate-semialdehyde dehydrogenase (CoA-acylating)
This is an abbreviated version!
For detailed information about methylmalonate-semialdehyde dehydrogenase (CoA-acylating), go to the full flat file.
Word Map on EC 1.2.1.27
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1.2.1.27
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lysosomotropic
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3-hydroxyisobutyrate
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coa-dependent
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mississippi
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propionyl-coa
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aldh6a1
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3-hydroxypropionic
- 1.2.1.27
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lysosomotropic
- 3-hydroxyisobutyrate
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coa-dependent
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mississippi
- propionyl-coa
- aldh6a1
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3-hydroxypropionic
Reaction
Synonyms
Aldh6a1, dddC, FG99_15390, KES23460, malonate-semialdehyde dehydrogenase, methylmalonate semialdehyde dehydrogenase, methylmalonate semialdehyde dehydrogenase protein, methylmalonate-semialdehyde dehydrogenase, methylmalonic acid semialdehyde dehydrogenase, MGG_01606, MMSADH, MMSDH, MoMSDH, MSDH, NAD-dependent malonate-semialdehyde dehydrogenase, OdoMMSDH, OsALDH6, PA3570, SSO1218
ECTree
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General Information
General Information on EC 1.2.1.27 - methylmalonate-semialdehyde dehydrogenase (CoA-acylating)
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evolution
malfunction
metabolism
physiological function
additional information
the enzyme is a member of the aldehyde dehydrogenase superfamily
evolution
evolutionary lineage history of Msdh across kingdoms, MSDH belongs to the aldehyde dehydrogenase (ALDH) superfamily of genes which are highly conserved and widely distributed in almost all organisms across kingdoms. In vivo expression pattern of Magnaporthe oryzae specific ALDH genes during host-pathogen interaction, overview
evolution
Pyricularia oryzae FGSC 8958
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evolutionary lineage history of Msdh across kingdoms, MSDH belongs to the aldehyde dehydrogenase (ALDH) superfamily of genes which are highly conserved and widely distributed in almost all organisms across kingdoms. In vivo expression pattern of Magnaporthe oryzae specific ALDH genes during host-pathogen interaction, overview
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evolution
Pyricularia oryzae ATCC MYA-4617
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evolutionary lineage history of Msdh across kingdoms, MSDH belongs to the aldehyde dehydrogenase (ALDH) superfamily of genes which are highly conserved and widely distributed in almost all organisms across kingdoms. In vivo expression pattern of Magnaporthe oryzae specific ALDH genes during host-pathogen interaction, overview
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evolution
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the enzyme is a member of the aldehyde dehydrogenase superfamily
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MSDH malfunction can be a reason for 3-hydroxyisobutyric aciduria, which is a disorder of valine metabolism
malfunction
MoMSDH deletion adversely affected the development of conidiophore and, as a result, conidiophore population as well as the number of conidia per conidiophore produced by the DELTAMomsdh deletion mutants are significantly reduced
malfunction
Pyricularia oryzae FGSC 8958
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MoMSDH deletion adversely affected the development of conidiophore and, as a result, conidiophore population as well as the number of conidia per conidiophore produced by the DELTAMomsdh deletion mutants are significantly reduced
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malfunction
Pyricularia oryzae ATCC MYA-4617
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MoMSDH deletion adversely affected the development of conidiophore and, as a result, conidiophore population as well as the number of conidia per conidiophore produced by the DELTAMomsdh deletion mutants are significantly reduced
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for MSDH, a major function in the degradation of branched chain amino acids is proposed which is supported by the high sequence homology with characterized MSDHs from bacteria
metabolism
contribution of the numerous ALDH genes to the fungal pathogenesis, 16 ALDH genes in Magnaporthe oryzae are idetified involved in infection and pathogenesis
metabolism
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for MSDH, a major function in the degradation of branched chain amino acids is proposed which is supported by the high sequence homology with characterized MSDHs from bacteria
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metabolism
Pyricularia oryzae FGSC 8958
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contribution of the numerous ALDH genes to the fungal pathogenesis, 16 ALDH genes in Magnaporthe oryzae are idetified involved in infection and pathogenesis
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metabolism
Pyricularia oryzae ATCC MYA-4617
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contribution of the numerous ALDH genes to the fungal pathogenesis, 16 ALDH genes in Magnaporthe oryzae are idetified involved in infection and pathogenesis
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the enzyme is involved in the decarboxylation of methylmalonate-semialdehyde (MMSA) downstream of the dimethylsulfoniopropionate (DMSP) cleavage pathway
physiological function
enzyme MoMsdh exerts minimal influence on the development of vegetative hyphae, but is involved in the regulation of conidiogenesis and conidiophoregenesis in Magnaporthe oryzae. Conidiation constitutes a pivotal developmental stage in fungal life-cycle and represents one of the most durable organs that promote fungal survival and facilitate their efficient dissemination. MoMsdh is involved in the regulating conditions necessary for promoting asexual reproductive development in Magnaporthe oryzae. MoMsdh is essential for pathogenicity of the organism. MoMsdh crucially regulates intracellular level of small branched-chain amino acids and appressoria mediating signalling molecules. MoMsdh specifically controls the localization of Spitzenkoerper in the conidium to ensure polarized speciation of germ tube. MoMsdh enhances membrane integrity by detoxifying alcohol and pyridoxine derived reactive osmolytes
physiological function
Pyricularia oryzae FGSC 8958
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enzyme MoMsdh exerts minimal influence on the development of vegetative hyphae, but is involved in the regulation of conidiogenesis and conidiophoregenesis in Magnaporthe oryzae. Conidiation constitutes a pivotal developmental stage in fungal life-cycle and represents one of the most durable organs that promote fungal survival and facilitate their efficient dissemination. MoMsdh is involved in the regulating conditions necessary for promoting asexual reproductive development in Magnaporthe oryzae. MoMsdh is essential for pathogenicity of the organism. MoMsdh crucially regulates intracellular level of small branched-chain amino acids and appressoria mediating signalling molecules. MoMsdh specifically controls the localization of Spitzenkoerper in the conidium to ensure polarized speciation of germ tube. MoMsdh enhances membrane integrity by detoxifying alcohol and pyridoxine derived reactive osmolytes
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physiological function
Pyricularia oryzae ATCC MYA-4617
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enzyme MoMsdh exerts minimal influence on the development of vegetative hyphae, but is involved in the regulation of conidiogenesis and conidiophoregenesis in Magnaporthe oryzae. Conidiation constitutes a pivotal developmental stage in fungal life-cycle and represents one of the most durable organs that promote fungal survival and facilitate their efficient dissemination. MoMsdh is involved in the regulating conditions necessary for promoting asexual reproductive development in Magnaporthe oryzae. MoMsdh is essential for pathogenicity of the organism. MoMsdh crucially regulates intracellular level of small branched-chain amino acids and appressoria mediating signalling molecules. MoMsdh specifically controls the localization of Spitzenkoerper in the conidium to ensure polarized speciation of germ tube. MoMsdh enhances membrane integrity by detoxifying alcohol and pyridoxine derived reactive osmolytes
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physiological function
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the enzyme is involved in the decarboxylation of methylmalonate-semialdehyde (MMSA) downstream of the dimethylsulfoniopropionate (DMSP) cleavage pathway
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identification of key residues important for substrate recognition and tetrahedral intermediate stabilization. Two basic residues (Arg103 and Arg279) and six hydrophobic residues (Phe150, Met153, Val154, Trp157, Met281, and Phe449) are important for tetrahedral intermediate binding. The backbone amide of Cys280 and the side chain amine of Asn149 function as the oxyanion hole during the enzymatic reaction
additional information
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identification of key residues important for substrate recognition and tetrahedral intermediate stabilization. Two basic residues (Arg103 and Arg279) and six hydrophobic residues (Phe150, Met153, Val154, Trp157, Met281, and Phe449) are important for tetrahedral intermediate binding. The backbone amide of Cys280 and the side chain amine of Asn149 function as the oxyanion hole during the enzymatic reaction
additional information
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identification of key residues important for substrate recognition and tetrahedral intermediate stabilization. Two basic residues (Arg103 and Arg279) and six hydrophobic residues (Phe150, Met153, Val154, Trp157, Met281, and Phe449) are important for tetrahedral intermediate binding. The backbone amide of Cys280 and the side chain amine of Asn149 function as the oxyanion hole during the enzymatic reaction
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