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Information on EC 1.2.1.27 - methylmalonate-semialdehyde dehydrogenase (CoA-acylating)
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1.2.1.27 methylmalonate-semialdehyde dehydrogenase (CoA-acylating)IUBMB Comments
Also converts 3-oxopropanoate into acetyl-CoA . The reaction occurs in two steps with the decarboxylation process preceding CoA-binding . Bicarbonate rather than CO2 is released as a final product .
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Word Map
- 1.2.1.27
-
lysosomotropic
- 3-hydroxyisobutyrate
-
coa-dependent
-
mississippi
- propionyl-coa
- aldh6a1
-
3-hydroxypropionic
The enzyme appears in viruses and cellular organisms
Synonyms
msdh, mmsdh, methylmalonate semialdehyde dehydrogenase, odommsdh, momsdh, methylmalonic acid semialdehyde dehydrogenase, mmsadh, sso1218, methylmalonate semialdehyde dehydrogenase protein, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
dddC
methylmalonate semialdehyde dehydrogenase
methylmalonate-semialdehyde dehydrogenase
MGG_01606
MMSDH
MoMSDH
MSDH
OdoMMSDH
SSO1218
MMSDH
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2-methyl-3-oxopropanoate + CoA + H2O + NAD+ = propanoyl-CoA + HCO3- + NADH
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
redox reaction
-
-
-
-
reduction
-
-
-
-
oxidation
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
-
,
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SYSTEMATIC NAME
IUBMB Comments
2-methyl-3-oxopropanoate:NAD+ 3-oxidoreductase (CoA-propanoylating)
Also converts 3-oxopropanoate into acetyl-CoA [3]. The reaction occurs in two steps with the decarboxylation process preceding CoA-binding [3]. Bicarbonate rather than CO2 is released as a final product [3].
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CAS REGISTRY NUMBER
COMMENTARY
37205-49-5
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
methylmalonate-semialdehyde + CoA + NAD+
propionyl-CoA + NADH + H+ + HCO3-
-
-
-
-
?
p-nitrophenyl acetate + CoA + NAD+
p-nitrophenol + acetyl-CoA + NADH
-
-
-
ir
propionaldehyde + CoA + H2O + NAD+
?
no physiological substrate
-
-
?
propionaldehyde + CoA + NAD+
? + NADH
highest activity, no physiological substrate for MSDH, it only forms the same thiopropionyl enzyme intermediate as methylmalonate semialdehyde and malonate semialdehyde
-
-
?
2-methyl-3-oxopropanoate + CoA + H2O + NAD+
propanoyl-CoA + HCO3- + NADH
-
-
-
?
2-methyl-3-oxopropanoate + CoA + H2O + NAD+
propanoyl-CoA + HCO3- + NADH
-
-
-
?
2-methyl-3-oxopropanoate + CoA + H2O + NAD+
propanoyl-CoA + HCO3- + NADH
-
-
-
?
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 + H2O + NAD+
propanoyl-CoA + HCO3- + NADH + H+
Pyricularia oryzae ATCC MYA-4617
-
-
-
?
2-methyl-3-oxopropanoate + CoA + H2O + NAD+
propanoyl-CoA + HCO3- + NADH + H+
Pyricularia oryzae FGSC 8958
-
-
-
?
2-methyl-3-oxopropanoate + CoA + NAD+
propanoyl-CoA + CO2 + NADH
-
-
-
-
?
2-methyl-3-oxopropanoate + CoA + NAD+
propanoyl-CoA + CO2 + NADH
-
-
-
?, ir
2-methyl-3-oxopropanoate + CoA + NAD+
propanoyl-CoA + CO2 + NADH
-
-
-
-
ir
2-methyl-3-oxopropanoate + CoA + NAD+
propanoyl-CoA + CO2 + NADH
-
other acyl acceptor: 2-mercaptoethanol
-
ir
2-methyl-3-oxopropanoate + CoA + NAD+
propanoyl-CoA + CO2 + NADH
-
other acyl acceptor: 2-mercaptoethanol
-
ir
2-methyl-3-oxopropanoate + CoA + NAD+
propanoyl-CoA + CO2 + NADH
-
other acyl acceptor: 2-mercaptoethanol
-
ir
2-methyl-3-oxopropanoate + CoA + NAD+
propanoyl-CoA + CO2 + NADH
-
-
-
-
ir
2-methyl-3-oxopropanoate + CoA + NAD+
propanoyl-CoA + CO2 + NADH
-
other acyl acceptor: 2-mercaptoethanol
-
ir
2-methyl-3-oxopropanoate + CoA + NAD+
propanoyl-CoA + CO2 + NADH
-
-
-
-
ir
2-methyl-3-oxopropanoate + CoA + NAD+
propanoyl-CoA + CO2 + NADH
-
both stereoisomers are oxidized
-
ir
malonate semialdehyde + CoA + H2O + NAD+
acetyl-CoA + CO2 + NADH
-
-
-
?
malonate semialdehyde + CoA + H2O + NAD+
acetyl-CoA + CO2 + NADH
-
-
-
?
malonate semialdehyde + CoA + NAD+
acetyl-CoA + CO2 + NADH
-
-
-
?
malonate semialdehyde + CoA + NAD+
acetyl-CoA + CO2 + NADH
-
-
-
?
methylmalonate semialdehyde + CoA + H2O + NAD+
propanoyl-CoA + HCO3- + NADH
-
-
-
-
?
methylmalonate semialdehyde + CoA + H2O + NAD+
propanoyl-CoA + HCO3- + NADH
weaker stabilization of the adenine ring triggers early NADH release in MSDH-catalyzed reaction
-
-
?
methylmalonate semialdehyde + CoA + H2O + NAD+
propanoyl-CoA + HCO3- + NADH
-
-
-
?
methylmalonate semialdehyde + CoA + H2O + NAD+
propanoyl-CoA + HCO3- + NADH
-
-
-
?
additional information
?
-
ALDH superfamily represents a group of enzymes that catalyze the oxidation of endogenous and exogenous aldehydes to the corresponding carboxylic acids
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
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
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
methylmalonate-semialdehyde + CoA + NAD+
propionyl-CoA + NADH + H+ + HCO3-
-
-
-
-
?
2-methyl-3-oxopropanoate + CoA + H2O + NAD+
propanoyl-CoA + HCO3- + NADH
-
-
-
?
2-methyl-3-oxopropanoate + CoA + H2O + NAD+
propanoyl-CoA + HCO3- + NADH
-
-
-
?
2-methyl-3-oxopropanoate + CoA + H2O + NAD+
propanoyl-CoA + HCO3- + NADH
-
-
-
?
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 + H2O + NAD+
propanoyl-CoA + HCO3- + NADH + H+
Pyricularia oryzae ATCC MYA-4617
-
-
-
?
2-methyl-3-oxopropanoate + CoA + H2O + NAD+
propanoyl-CoA + HCO3- + NADH + H+
Pyricularia oryzae FGSC 8958
-
-
-
?
2-methyl-3-oxopropanoate + CoA + NAD+
propanoyl-CoA + CO2 + NADH
-
-
-
-
ir
2-methyl-3-oxopropanoate + CoA + NAD+
propanoyl-CoA + CO2 + NADH
-
-
-
-
ir
2-methyl-3-oxopropanoate + CoA + NAD+
propanoyl-CoA + CO2 + NADH
-
-
-
-
ir
additional information
?
-
ALDH superfamily represents a group of enzymes that catalyze the oxidation of endogenous and exogenous aldehydes to the corresponding carboxylic acids
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NAD+
-
the central beta-sheet of five strands surrounded by alpha-helices in the first domain forming the cofactor-binding site, including residues 39-248, minus the extension of residues 119-136
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Acquired Immunodeficiency Syndrome
Quality of life of men with AIDS and the model of social determinants of health.
HIV Infections
HIV infection among young black men who have sex with men--Jackson, Mississippi, 2006-2008.
methylmalonate-semialdehyde dehydrogenase (coa-acylating) deficiency
3-Hydroxyisobutyrate aciduria and mutations in the ALDH6A1 gene coding for methylmalonate semialdehyde dehydrogenase.
methylmalonate-semialdehyde dehydrogenase (coa-acylating) deficiency
Clinical, biochemical, mitochondrial, and metabolomic aspects of methylmalonate semialdehyde dehydrogenase deficiency: Report of a fifth case.
methylmalonate-semialdehyde dehydrogenase (coa-acylating) deficiency
Molecular characterization of methylmalonate semialdehyde dehydrogenase deficiency.
Neoplasms
Establishment of Patient-derived Succinate Dehydrogenase-deficient Gastrointestinal Stromal Tumor Models For Predicting Therapeutic Response.
Neoplasms
Identification of ALDH6A1 as a Potential Molecular Signature in Hepatocellular Carcinoma via Quantitative Profiling of the Mitochondrial Proteome.
Syphilis
Integrating HIV testing into syphilis partner services in Mississippi to improve HIV case finding.
Syphilis
Integrating Human Immunodeficiency Virus Testing Into Syphilis Partner Services in Mississippi to Improve Human Immunodeficiency Virus Case Finding.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
-
0.06
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
0.085
CoA
-
wild type MSDH, steady-state conditions with propionaldehyde, 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, steady-state conditions with methylmalonate semialdehyde, pH 8.2 and 30°C
0.33
CoA
-
R124L mutant enzyme, steady-state conditions with propionaldehyde, 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
0.023
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
0.06
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
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, steady-state conditions with methylmalonate semialdehyde, pH 8.2 and 30°C
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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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
Kcat-value of CoA for R301L mutant enzyme under steady-state conditions with propionaldehyde is above 3 1/sec at pH 8.2 and 30°C
-
1.1
2-Methyl-3-oxopropanoate
-
50 mM potassium phosphate pH 8.2, 30°C, 0.5 mM 2-methyl-3-oxopropanoate, 12 mM NAD+, 0.5 mM CoA
2.8
CoA
-
R124L mutant enzyme, steady-state conditions with propionaldehyde, pH 8.2 and 30°C
12.6
CoA
-
wild type MSDH, 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
0.14
NAD+
-
R301L mutant enzyme, steady-state conditions with methylmalonate semialdehyde, pH 8.2 and 30°C
2.2
NAD+
-
wild type MSDH, steady-state conditions with methylmalonate semialdehyde, pH 8.2 and 30°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3
CoA
-
R301L mutant enzyme, steady-state conditions with propionaldehyde, pH 8.2 and 30°C
8.5
CoA
-
R124L mutant enzyme, steady-state conditions with propionaldehyde, pH 8.2 and 30°C
150
CoA
-
wild type MSDH, steady-state conditions with propionaldehyde, pH 8.2 and 30°C
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE