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2-methyl-3-oxopropanoate + CoA + H2O + NAD+
propanoyl-CoA + HCO3- + NADH
2-methyl-3-oxopropanoate + CoA + H2O + NAD+
propanoyl-CoA + HCO3- + NADH + H+
2-methyl-3-oxopropanoate + CoA + NAD+
propanoyl-CoA + CO2 + NADH
2-methylbutyraldehyde + CoA + NAD+
?
-
Substrates: low activity
Products: -
?
acetaldehyde + CoA + NAD+
?
-
Substrates: low activity
Products: -
?
butyraldehyde + CoA + NAD+
?
-
Substrates: low activity
Products: -
?
isobutyraldehyde + CoA + NAD+
?
-
Substrates: low activity
Products: -
?
malonate semialdehyde + CoA + H2O + NAD+
acetyl-CoA + CO2 + NADH
malonate semialdehyde + CoA + NAD+
acetyl-CoA + CO2 + NADH
malondialdehyde + CoA + NAD+
?
-
Substrates: low activity
Products: -
?
methylmalonate semialdehyde + CoA + H2O + NAD+
propanoyl-CoA + HCO3- + NADH
methylmalonate-semialdehyde + CoA + NAD+
propionyl-CoA + NADH + H+ + HCO3-
-
Substrates: -
Products: -
?
p-nitrophenyl acetate + CoA + NAD+
p-nitrophenol + acetyl-CoA + NADH
-
Substrates: -
Products: -
ir
propanal + 2-mercaptoethanol + NAD+
? + NADH
propanal + CoA + NAD+
propanoyl-CoA + NADH
-
Substrates: -
Products: -
ir
propanal + NAD+
? + NADH
-
Substrates: -
Products: -
?
propionaldehyde + CoA + H2O + NAD+
?
Substrates: no physiological substrate
Products: -
?
propionaldehyde + CoA + NAD+
? + NADH
Substrates: highest activity, no physiological substrate for MSDH, it only forms the same thiopropionyl enzyme intermediate as methylmalonate semialdehyde and malonate semialdehyde
Products: -
?
propionaldehyde + CoA + NAD+
propanoyl-CoA + NADH
-
Substrates: -
Products: -
?
succinate semialdehyde + CoA + NAD+
?
-
Substrates: very low activity
Products: -
?
additional information
?
-
2-methyl-3-oxopropanoate + CoA + H2O + NAD+
propanoyl-CoA + HCO3- + NADH
Substrates: -
Products: -
?
2-methyl-3-oxopropanoate + CoA + H2O + NAD+
propanoyl-CoA + HCO3- + NADH
Substrates: -
Products: -
?
2-methyl-3-oxopropanoate + CoA + H2O + NAD+
propanoyl-CoA + HCO3- + NADH
Substrates: -
Products: -
?
2-methyl-3-oxopropanoate + CoA + H2O + NAD+
propanoyl-CoA + HCO3- + NADH
Substrates: -
Products: -
?
2-methyl-3-oxopropanoate + CoA + H2O + NAD+
propanoyl-CoA + HCO3- + NADH + H+
Substrates: -
Products: -
?
2-methyl-3-oxopropanoate + CoA + H2O + NAD+
propanoyl-CoA + HCO3- + NADH + H+
Substrates: -
Products: -
?
2-methyl-3-oxopropanoate + CoA + H2O + NAD+
propanoyl-CoA + HCO3- + NADH + H+
Substrates: -
Products: -
?
2-methyl-3-oxopropanoate + CoA + NAD+
propanoyl-CoA + CO2 + NADH
-
Substrates: -
Products: -
?
2-methyl-3-oxopropanoate + CoA + NAD+
propanoyl-CoA + CO2 + NADH
Substrates: -
Products: -
?, ir
2-methyl-3-oxopropanoate + CoA + NAD+
propanoyl-CoA + CO2 + NADH
-
Substrates: -
Products: -
ir
2-methyl-3-oxopropanoate + CoA + NAD+
propanoyl-CoA + CO2 + NADH
-
Substrates: -
Products: -
ir
2-methyl-3-oxopropanoate + CoA + NAD+
propanoyl-CoA + CO2 + NADH
-
Substrates: other acyl acceptor: 2-mercaptoethanol
Products: -
ir
2-methyl-3-oxopropanoate + CoA + NAD+
propanoyl-CoA + CO2 + NADH
-
Substrates: -
Products: -
ir
2-methyl-3-oxopropanoate + CoA + NAD+
propanoyl-CoA + CO2 + NADH
-
Substrates: other acyl acceptor: 2-mercaptoethanol
Products: -
ir
2-methyl-3-oxopropanoate + CoA + NAD+
propanoyl-CoA + CO2 + NADH
-
Substrates: -
Products: -
ir
2-methyl-3-oxopropanoate + CoA + NAD+
propanoyl-CoA + CO2 + NADH
-
Substrates: both stereoisomers are oxidized
Products: -
ir
malonate semialdehyde + CoA + H2O + NAD+
acetyl-CoA + CO2 + NADH
Substrates: -
Products: -
?
malonate semialdehyde + CoA + H2O + NAD+
acetyl-CoA + CO2 + NADH
Substrates: -
Products: -
?
malonate semialdehyde + CoA + NAD+
acetyl-CoA + CO2 + NADH
-
Substrates: -
Products: -
?
malonate semialdehyde + CoA + NAD+
acetyl-CoA + CO2 + NADH
-
Substrates: -
Products: -
?
malonate semialdehyde + CoA + NAD+
acetyl-CoA + CO2 + NADH
-
Substrates: -
Products: -
ir
malonate semialdehyde + CoA + NAD+
acetyl-CoA + CO2 + NADH
Substrates: -
Products: -
?
malonate semialdehyde + CoA + NAD+
acetyl-CoA + CO2 + NADH
Substrates: -
Products: -
?
methylmalonate semialdehyde + CoA + H2O + NAD+
propanoyl-CoA + HCO3- + NADH
-
Substrates: -
Products: -
?
methylmalonate semialdehyde + CoA + H2O + NAD+
propanoyl-CoA + HCO3- + NADH
Substrates: weaker stabilization of the adenine ring triggers early NADH release in MSDH-catalyzed reaction
Products: -
?
methylmalonate semialdehyde + CoA + H2O + NAD+
propanoyl-CoA + HCO3- + NADH
Substrates: -
Products: -
?
methylmalonate semialdehyde + CoA + H2O + NAD+
propanoyl-CoA + HCO3- + NADH
Substrates: -
Products: -
?
propanal + 2-mercaptoethanol + NAD+
? + NADH
-
Substrates: -
Products: -
ir
propanal + 2-mercaptoethanol + NAD+
? + NADH
-
Substrates: -
Products: -
ir
additional information
?
-
Substrates: ALDH superfamily represents a group of enzymes that catalyze the oxidation of endogenous and exogenous aldehydes to the corresponding carboxylic acids
Products: -
?
additional information
?
-
-
Substrates: the malonate-semialdehyde dehydrogenase is selective towards malonate semialdehyde and generates acetyl-CoA in an NAD-dependent and CoA-dependent reaction, although a slower CoA-independent reaction generating acetate is also observed
Products: -
?
additional information
?
-
-
Substrates: the malonate-semialdehyde dehydrogenase is selective towards malonate semialdehyde and generates acetyl-CoA in an NAD-dependent and CoA-dependent reaction, although a slower CoA-independent reaction generating acetate is also observed
Products: -
?
additional information
?
-
Substrates: no activity is observed for the substrates D,L-glyceraldehyde, D,L-glyceraldehyde 3-phosphate and D,L-glycolaldehyde neither with NAD+ nor with NADP+ as cosubstrate
Products: -
?
additional information
?
-
-
Substrates: no activity is observed for the substrates D,L-glyceraldehyde, D,L-glyceraldehyde 3-phosphate and D,L-glycolaldehyde neither with NAD+ nor with NADP+ as cosubstrate
Products: -
?
additional information
?
-
Substrates: no activity detected in the presence of NADP+ as cosubstrate, no activity with D,L-glyceraldehyde, D,L-glyceraldehyde-3-phosphate and D,L-glycolaldehyde - neither with NAD+ nor with NADP+ as cosubstrate
Products: -
?
additional information
?
-
-
Substrates: no activity detected in the presence of NADP+ as cosubstrate, no activity with D,L-glyceraldehyde, D,L-glyceraldehyde-3-phosphate and D,L-glycolaldehyde - neither with NAD+ nor with NADP+ as cosubstrate
Products: -
?
additional information
?
-
Substrates: no activity is observed for the substrates D,L-glyceraldehyde, D,L-glyceraldehyde 3-phosphate and D,L-glycolaldehyde neither with NAD+ nor with NADP+ as cosubstrate
Products: -
?
additional information
?
-
Substrates: no activity detected in the presence of NADP+ as cosubstrate, no activity with D,L-glyceraldehyde, D,L-glyceraldehyde-3-phosphate and D,L-glycolaldehyde - neither with NAD+ nor with NADP+ as cosubstrate
Products: -
?
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2-methyl-3-oxopropanoate + CoA + H2O + NAD+
propanoyl-CoA + HCO3- + NADH
2-methyl-3-oxopropanoate + CoA + H2O + NAD+
propanoyl-CoA + HCO3- + NADH + H+
2-methyl-3-oxopropanoate + CoA + NAD+
propanoyl-CoA + CO2 + NADH
malonate semialdehyde + CoA + NAD+
acetyl-CoA + CO2 + NADH
-
Substrates: -
Products: -
ir
methylmalonate-semialdehyde + CoA + NAD+
propionyl-CoA + NADH + H+ + HCO3-
-
Substrates: -
Products: -
?
additional information
?
-
2-methyl-3-oxopropanoate + CoA + H2O + NAD+
propanoyl-CoA + HCO3- + NADH
Substrates: -
Products: -
?
2-methyl-3-oxopropanoate + CoA + H2O + NAD+
propanoyl-CoA + HCO3- + NADH
Substrates: -
Products: -
?
2-methyl-3-oxopropanoate + CoA + H2O + NAD+
propanoyl-CoA + HCO3- + NADH
Substrates: -
Products: -
?
2-methyl-3-oxopropanoate + CoA + H2O + NAD+
propanoyl-CoA + HCO3- + NADH
Substrates: -
Products: -
?
2-methyl-3-oxopropanoate + CoA + H2O + NAD+
propanoyl-CoA + HCO3- + NADH + H+
Substrates: -
Products: -
?
2-methyl-3-oxopropanoate + CoA + H2O + NAD+
propanoyl-CoA + HCO3- + NADH + H+
Substrates: -
Products: -
?
2-methyl-3-oxopropanoate + CoA + H2O + NAD+
propanoyl-CoA + HCO3- + NADH + H+
Substrates: -
Products: -
?
2-methyl-3-oxopropanoate + CoA + NAD+
propanoyl-CoA + CO2 + NADH
-
Substrates: -
Products: -
?
2-methyl-3-oxopropanoate + CoA + NAD+
propanoyl-CoA + CO2 + NADH
Substrates: -
Products: -
?
2-methyl-3-oxopropanoate + CoA + NAD+
propanoyl-CoA + CO2 + NADH
-
Substrates: -
Products: -
ir
2-methyl-3-oxopropanoate + CoA + NAD+
propanoyl-CoA + CO2 + NADH
-
Substrates: -
Products: -
ir
2-methyl-3-oxopropanoate + CoA + NAD+
propanoyl-CoA + CO2 + NADH
-
Substrates: -
Products: -
ir
additional information
?
-
Substrates: ALDH superfamily represents a group of enzymes that catalyze the oxidation of endogenous and exogenous aldehydes to the corresponding carboxylic acids
Products: -
?
additional information
?
-
-
Substrates: the malonate-semialdehyde dehydrogenase is selective towards malonate semialdehyde and generates acetyl-CoA in an NAD-dependent and CoA-dependent reaction, although a slower CoA-independent reaction generating acetate is also observed
Products: -
?
additional information
?
-
-
Substrates: the malonate-semialdehyde dehydrogenase is selective towards malonate semialdehyde and generates acetyl-CoA in an NAD-dependent and CoA-dependent reaction, although a slower CoA-independent reaction generating acetate is also observed
Products: -
?
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0.54 - 44
2-mercaptoethanol
0.0025 - 0.06
2-Methyl-3-oxopropanoate
0.0045
malonate semialdehyde
-
-
0.006 - 0.215
methylmalonate semialdehyde
9.3 - 9.8
propionaldehyde
additional information
additional information
-
Km-value of CoA for R301L mutant enzyme under steady-state conditions with propionaldehyde is above 1 mM at pH 8.2 and 30°C
-
0.54
2-mercaptoethanol
-
-
0.0025
2-Methyl-3-oxopropanoate
-
-
0.0053
2-Methyl-3-oxopropanoate
-
-
0.019
2-Methyl-3-oxopropanoate
-
-
0.024
2-Methyl-3-oxopropanoate
-
-
0.06
2-Methyl-3-oxopropanoate
-
50 mM KP04 pH 8.2, 30°C, 0.5 mM 2-methyl-3-oxopropanoate, 12 mM NAD+, 0.5 mM CoA
0.021
CoA
-
-
0.063
CoA
V229G/G225 insertion, pH 8.2 and 30°C
0.085
CoA
-
wild type MSDH, steady-state conditions with propionaldehyde, pH 8.2 and 30°C
0.096
CoA
V229G/H226P/G225 insertion, pH 8.2 and 30°C
0.119
CoA
V229G/H226P, pH 8.2 and 30°C
0.12
CoA
-
50 mM potassium phosphate pH 8.2, 30°C, 0.5 mM 2-methyl-3-oxopropanoate, 12 mM NAD+, 0.5 mM CoA
0.12
CoA
wild type MSDH, pH 8.2 and 30°C
0.12
CoA
-
wild type MSDH, steady-state conditions with methylmalonate semialdehyde, pH 8.2 and 30°C
0.151
CoA
G225 insertion, pH 8.2 and 30°C
0.234
CoA
V229G, pH 8.2 and 30°C
0.33
CoA
-
R124L mutant enzyme, steady-state conditions with propionaldehyde, pH 8.2 and 30°C
0.497
CoA
V229G/Y252L/V253I/G225 insertion, pH 8.2 and 30°C
0.57
CoA
-
R124L mutant enzyme, steady-state conditions with methylmalonate semialdehyde, pH 8.2 and 30°C
0.62
CoA
-
R301L mutant enzyme, steady-state conditions with methylmalonate semialdehyde, pH 8.2 and 30°C
0.006
methylmalonate semialdehyde
-
R124L mutant enzyme, steady-state conditions, pH 8.2 and 30°C
0.021
methylmalonate semialdehyde
V229G/H226P/G225 insertion, pH 8.2 and 30°C
0.022
methylmalonate semialdehyde
G225 insertion, pH 8.2 and 30°C
0.023
methylmalonate semialdehyde
-
R301L mutant enzyme, steady-state conditions, pH 8.2 and 30°C
0.027
methylmalonate semialdehyde
V229G/G225 insertion, pH 8.2 and 30°C
0.028
methylmalonate semialdehyde
V229G/H226P, pH 8.2 and 30°C
0.054
methylmalonate semialdehyde
V229G, pH 8.2 and 30°C
0.06
methylmalonate semialdehyde
wild type MSDH, pH 8.2 and 30°C
0.06
methylmalonate semialdehyde
-
wild type MSDH, steady-state conditions, pH 8.2 and 30°C
0.215
methylmalonate semialdehyde
V229G/Y252L/V253I/G225 insertion, pH 8.2 and 30°C
0.033
NAD+
-
wild type MSDH, steady-state conditions with propionaldehyde, pH 8.2 and 30°C
0.038
NAD+
-
R124L mutant enzyme, steady-state conditions with propionaldehyde, pH 8.2 and 30°C
0.06
NAD+
-
R124L mutant enzyme, steady-state conditions with methylmalonate semialdehyde, pH 8.2 and 30°C
0.12
NAD+
-
R301L mutant enzyme, steady-state conditions with methylmalonate semialdehyde, pH 8.2 and 30°C
0.15
NAD+
V229G/G225 insertion, pH 8.2 and 30°C
0.57
NAD+
V229G, pH 8.2 and 30°C
0.66
NAD+
V229G/H226P, pH 8.2 and 30°C
0.69
NAD+
G225 insertion, pH 8.2 and 30°C
0.77
NAD+
V229G/H226P/G225 insertion, pH 8.2 and 30°C
2.3
NAD+
-
50 mM potassium phosphate pH 8.2, 30°C, 0.5 mM 2-methyl-3-oxopropanoate, 12 mM NAD+, 0.5 mM CoA
2.3
NAD+
wild type MSDH, pH 8.2 and 30°C
2.3
NAD+
-
wild type MSDH, steady-state conditions with methylmalonate semialdehyde, pH 8.2 and 30°C
9.44
NAD+
V229G/Y252L/V253I/G225 insertion, pH 8.2 and 30°C
6.1
propanal
-
-
9.3
propionaldehyde
-
R124L mutant enzyme, steady-state conditions, pH 8.2 and 30°C
9.8
propionaldehyde
-
wild type MSDH, steady-state conditions, pH 8.2 and 30°C
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evolution
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
-
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
-
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
-
the enzyme is a member of the aldehyde dehydrogenase superfamily
-
malfunction
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
-
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
-
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
-
metabolism
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
MSDH enzyme is part of the catabolism pathway of L-valine
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
-
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
-
contribution of the numerous ALDH genes to the fungal pathogenesis, 16 ALDH genes in Magnaporthe oryzae are idetified involved in infection and pathogenesis
-
physiological function
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
-
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
-
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
-
the enzyme is involved in the decarboxylation of methylmalonate-semialdehyde (MMSA) downstream of the dimethylsulfoniopropionate (DMSP) cleavage pathway
-
additional information
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
-
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
-
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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dimer
-
2 * 58000, SDS-PAGE
dimer
-
2 * 69000, gel filtration in presence of SDS
homodimer
2 * 54000, SDS-PAGE, in solution
homodimer
-
2 * 54000, SDS-PAGE, in solution
-
tetramer
dimer of dimers, monomer consists of three domains, the dinucleotide binding domain comprising the residues 3123 and 141251, the catalytic domain with residues 252270, and a small domain, with residues 124140 and 471486
tetramer
-
the monomeric structure is made up of two primary domains. Each has a central extended beta-sheet surrounded by alpha-helices, with a cleft between them which holds the cofactor. The second primary domain extends from residues 249 to 444 and has a central beta-sheet of seven strands surrounded by alpha-helices. This second beta-sheet is extended by the three beta-strands of the neighbouring dimer extension (residues 119-136 and 444-494) to make a beta-sheet of ten strands in the dimer structure. The finger extension (residues 119-136 and 444-480) forms a three-stranded beta-sheet extension which pulls the dimer structure together, but is also used as a hook to pull in a neighbouring dimer and form the basis of the hexameric structure
tetramer
-
the monomeric structure is made up of two primary domains. Each has a central extended beta-sheet surrounded by alpha-helices, with a cleft between them which holds the cofactor. The second primary domain extends from residues 249 to 444 and has a central beta-sheet of seven strands surrounded by alpha-helices. This second beta-sheet is extended by the three beta-strands of the neighbouring dimer extension (residues 119-136 and 444-494) to make a beta-sheet of ten strands in the dimer structure. The finger extension (residues 119-136 and 444-480) forms a three-stranded beta-sheet extension which pulls the dimer structure together, but is also used as a hook to pull in a neighbouring dimer and form the basis of the hexameric structure
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tetramer
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4 * 58000, SDS-PAGE
tetramer
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4 * 55330, cDNA sequence
additional information
each subunit consists of three distinct domains: an NAD-binding domain, a catalytic domain, and an oligomerization domain. 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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each subunit consists of three distinct domains: an NAD-binding domain, a catalytic domain, and an oligomerization domain. 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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each subunit consists of three distinct domains: an NAD-binding domain, a catalytic domain, and an oligomerization domain. 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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additional information
MoMsdh domain architecture, overview
additional information
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MoMsdh domain architecture, overview
additional information
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MoMsdh domain architecture, overview
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additional information
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MoMsdh domain architecture, overview
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C49A/C176A/C305A/C369A/C403A
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kinetic parameters similar to the wild-type enzmye
N427L
substitution dramatically alters the catalytic properties of the enzyme, acylation becomes rate-limiting with a decrease of the associated rate constant by at least 10000fold relative to the wild-type MSDH
R124L
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results obtained under pre-steady conditions show that both Arg residues participate not only in methylmalonate semialdehyde binding via stabilizing interactions between the guanidinium groups and the carboxylate but also in the formation of an efficient MSDH-NAD+-methylmalonate semialdehyde ternary complex
R301L
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results obtained under pre-steady conditions show that both Arg residues participate not only in methylmalonate semialdehyde binding via stabilizing interactions between the guanidinium groups and the carboxylate but also in the formation of an efficient MSDH-NAD+-methylmalonate semialdehyde ternary complex
V229G/Y252L/V253I
together with insertion of glycine at position 225, rate-limiting step changes to acylation instead of deacylation
W177F
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NAD-binding followed by fluorescence quenching of methylmalonate semialdehyde dehydrogenase. Only W468 is responsible for time-dependent additional quenching
W28F
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NAD-binding followed by fluorescence quenching of methylmalonate semialdehyde dehydrogenase. Only W468 is responsible for time-dependent additional quenching
W397F
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NAD-binding followed by fluorescence quenching of methylmalonate semialdehyde dehydrogenase. Only W468 is responsible for time-dependent additional quenching
W468F
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NAD-binding followed by fluorescence quenching of methylmalonate semialdehyde dehydrogenase. Only W468 is responsible for time-dependent additional quenching
W76F
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NAD-binding followed by fluorescence quenching of methylmalonate semialdehyde dehydrogenase. Only W468 is responsible for time-dependent additional quenching
P62S
missense mutation in a highly conserved amino acid of MSDH, patient has severe developmental delay associated with development of marked post-natal microcephaly, at 7 years static moderate learning difficulties and borderline microcephaly
S262Y
missense mutation in a highly conserved amino acid of MSDH, patient developed a febrile illness and died from a hepatoencephalopathy at 2 years of age
C285A
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expressed in Escherichia coli, no activity
N251E
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expressed in Escherichia coli, no activity
V229G
significant decrease of the rate constant associated with the dissociation of NADH from the NADH-thioacylenzyme complex
V229G
together with insertion of glycine at position 225, significant decrease of the rate constant associated with the dissociation of NADH from the NADH/thioacylenzyme complex
V229G/H226P
rate-limiting step changes to acylation instead of deacylation
V229G/H226P
together with insertion of glycine at position 225, rate-limiting step changes to acylation instead of deacylation
additional information
further mutant enzyme created by single insertion of glycine at position 225 resulting in significant decrease of the rate constant associated with the dissociation of NADH fromthe NADH/thioacylenzyme complex
additional information
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further mutant enzyme created by single insertion of glycine at position 225 resulting in significant decrease of the rate constant associated with the dissociation of NADH fromthe NADH/thioacylenzyme complex
additional information
DELTAMomsdh mutant, constructed by DNA targeted replacement of MoMSDH, produces only few restricted lesion on host tissues, MoMSDH deletion accounts for the drastic reduction in lesion size by rendering the DELTAMomsdh mutants incapable of mobilizing the necessary energy required to effectively colonize host tissues. DELTAMomsdh deletion mutants exhibit higher intracellular level of amino acids Val, Leu, Ile, and of pyridoxine
additional information
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DELTAMomsdh mutant, constructed by DNA targeted replacement of MoMSDH, produces only few restricted lesion on host tissues, MoMSDH deletion accounts for the drastic reduction in lesion size by rendering the DELTAMomsdh mutants incapable of mobilizing the necessary energy required to effectively colonize host tissues. DELTAMomsdh deletion mutants exhibit higher intracellular level of amino acids Val, Leu, Ile, and of pyridoxine
additional information
-
DELTAMomsdh mutant, constructed by DNA targeted replacement of MoMSDH, produces only few restricted lesion on host tissues, MoMSDH deletion accounts for the drastic reduction in lesion size by rendering the DELTAMomsdh mutants incapable of mobilizing the necessary energy required to effectively colonize host tissues. DELTAMomsdh deletion mutants exhibit higher intracellular level of amino acids Val, Leu, Ile, and of pyridoxine
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additional information
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DELTAMomsdh mutant, constructed by DNA targeted replacement of MoMSDH, produces only few restricted lesion on host tissues, MoMSDH deletion accounts for the drastic reduction in lesion size by rendering the DELTAMomsdh mutants incapable of mobilizing the necessary energy required to effectively colonize host tissues. DELTAMomsdh deletion mutants exhibit higher intracellular level of amino acids Val, Leu, Ile, and of pyridoxine
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Goodwin, G.W.; Rougraff, P.M.; Davis, E.J.; Harris, R.A.
Purification and characterization of methylmalonate-semialdehyde dehydrogenase from rat liver. Identity to malonate-semialdehyde dehydrogenase
J. Biol. Chem.
264
14965-14971
1989
Rattus norvegicus
brenda
Hatter, K.; Sokatch, J.R.
Purification of methylmalonate-semialdehyde dehydrogenase from Pseudomonas aeruginosa PAO
Methods Enzymol.
166
389-393
1988
Homo sapiens, Pseudomonas aeruginosa, Pseudomonas aeruginosa PAO
brenda
Bannerjee, D.; Sanders, L.E.; Sokatch, J.R.
Properties of purified methylmalonate semialdehyde dehydrogenase of Pseudomonas aeruginosa
J. Biol. Chem.
245
1828-1835
1970
Pseudomonas aeruginosa
brenda
Sokatch, J.R.; Sanders, L.E.; Marshall, V.P.
Oxidation of methylmalonate semialdehyde to propionyl coenzyme A in Pseudomonas aeruginosa grown on valine
J. Biol. Chem.
243
2500-2506
1968
Pseudomonas aeruginosa
brenda
Harris, R.A.; Popov, K.M.; Kedishvili, N.Y.; Zhao, Y.; Shimomura, Y.; Robbins, B.; Crabb, D.W.
Molecular cloning of the branched-chain.alpha-keto acid dehydrogenase kinase and the CoA-dependent methylmalonate semialdehyde dehydrogenase
Adv. Enzyme Regul.
33
255-265
1993
Rattus norvegicus
brenda
Zhang, Y.X.; Tang, L.; Hutchinson, C.R.
Cloning and characterization of a gene (msdA) encoding methylmalonic acid semialdehyde dehydrogenase from Streptomyces coelicolor
J. Bacteriol.
178
490-495
1996
Streptomyces coelicolor
brenda
Kedishvili, N.Y.; Goodwin, G.W.; Popov, K.M.; Harris, R.A.
Mammalian methylmalonate-semialdehyde dehydrogenase
Methods Enzymol.
324
207-218
2000
Homo sapiens, Rattus norvegicus
brenda
Dubourg, H.; Stines-Chaumeil, C.; Didierjean, C.; Talfournier, F.; Rahuel-Clermont, S.; Branlant, G.; Aubry, A.
Expression, purification, crystallization and preliminary X-ray diffraction data of methylmalonate-semialdehyde dehydrogenase from Bacillus subtilis
Acta Crystallogr. Sect. D
60
1435-1437
2004
Bacillus subtilis
brenda
Oguchi, K.; Tanaka, N.; Komatsu, S.; Akao, S.
Methylmalonate-semialdehyde dehydrogenase is induced in auxin-stimulated and zinc-stimulated root formation in rice
Plant Cell Rep.
22
848-858
2004
Oryza sativa (O49218), Oryza sativa
brenda
Stines-Chaumeil, C.; Talfournier, F.; Branlant, G.
Mechanistic characterization of the MSDH (methylmalonate semialdehyde dehydrogenase) from Bacillus subtilis
Biochem. J.
395
107-115
2006
Bacillus subtilis
brenda
Li, C.; Akopiants, K.; Reynolds, K.A.
Identification and disruptional analysis of the Streptomyces cinnamonensis msdA gene, encoding methylmalonic acid semialdehyde dehydrogenase
J. Ind. Microbiol. Biotechnol.
33
75-83
2006
Streptomyces virginiae
brenda
Tanaka, N.; Takahashi, H.; Kitano, H.; Matsuoka, M.; Akao, S.; Uchimiya, H.; Komatsu, S.
Proteome approach to characterize the methylmalonate-semialdehyde dehydrogenase that is regulated by gibberellin
J. Proteome Res.
4
1575-1582
2005
Oryza sativa, Oryza sativa Japonica
brenda
Gao, C.; Han, B.
Evolutionary and expression study of the aldehyde dehydrogenase (ALDH) gene superfamily in rice (Oryza sativa)
Gene
431
86-94
2009
Oryza sativa (Q6Z4E4)
brenda
Su, H.C.; Ramkissoon, K.; Doolittle, J.; Clark, M.; Khatun, J.; Secrest, A.; Wolfgang, M.C.; Giddings, M.C.
The development of ciprofloxacin resistance in Pseudomonas aeruginosa involves multiple response stages and multiple proteins
Antimicrob. Agents Chemother.
54
4626-4635
2010
Pseudomonas aeruginosa
brenda
Esser, D.; Kouril, T.; Talfournier, F.; Polkowska, J.; Schrader, T.; Brsen, C.; Siebers, B.
Unraveling the function of paralogs of the aldehyde dehydrogenase super family from Sulfolobus solfataricus
Extremophiles
17
205-216
2013
Saccharolobus solfataricus (Q97YT9), Saccharolobus solfataricus, Saccharolobus solfataricus P2 (Q97YT9)
brenda
Talfournier, F.; Stines-Chaumeil, C.; Branlant, G.
Methylmalonate-semialdehyde dehydrogenase from Bacillus subtilis: substrate specificity and coenzyme A binding
J. Biol. Chem.
286
21971-21981
2011
Bacillus subtilis
brenda
Bchini, R.; Dubourg-Gerecke, H.; Rahuel-Clermont, S.; Aubry, A.; Branlant, G.; Didierjean, C.; Talfournier, F.
Adenine binding mode is a key factor in triggering the early release of NADH in coenzyme A-dependent methylmalonate semialdehyde dehydrogenase
J. Biol. Chem.
287
31095-31103
2012
Bacillus subtilis (P42412), Bacillus subtilis
brenda
Sass, J.O.; Walter, M.; Shield, J.P.; Atherton, A.M.; Garg, U.; Scott, D.; Woods, C.G.; Smith, L.D.
3-Hydroxyisobutyrate aciduria and mutations in the ALDH6A1 gene coding for methylmalonate semialdehyde dehydrogenase
J. Inherit. Metab. Dis.
35
437-442
2012
Homo sapiens (Q02252), Homo sapiens
brenda
Wilding, M.; Scott, C.; Peat, T.S.; Newman, J.
X-ray crystal structure of a malonate-semialdehyde dehydrogenase from Pseudomonas sp. strain AAC
Acta Crystallogr. Sect. F
73
24-28
2017
Pseudomonas sp., Pseudomonas sp. AAC
brenda
Do, H.; Lee, C.W.; Lee, S.G.; Kang, H.; Park, C.M.; Kim, H.J.; Park, H.; Park, H.; Lee, J.H.
Crystal structure and modeling of the tetrahedral intermediate state of methylmalonate-semialdehyde dehydrogenase (MMSDH) from Oceanimonas doudoroffii
J. Microbiol.
54
114-121
2016
Oceanimonas doudoroffii (G5CZI2), Oceanimonas doudoroffii, Oceanimonas doudoroffii ATCC 27123 (G5CZI2)
brenda
Norvienyeku, J.; Zhong, Z.; Lin, L.; Dang, X.; Chen, M.; Lin, X.; Zhang, H.; Anjago, W.M.; Lin, L.; Abdul, W.; Wang, Z.
Methylmalonate-semialdehyde dehydrogenase mediated metabolite homeostasis essentially regulate conidiation, polarized germination and pathogenesis in Magnaporthe oryzae
Environ. Microbiol.
19
4256-4277
2017
Pyricularia oryzae (G4MTY9), Pyricularia oryzae, Pyricularia oryzae ATCC MYA-4617 (G4MTY9), Pyricularia oryzae FGSC 8958 (G4MTY9)
brenda