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
1.2.1.27 methylmalonate-semialdehyde dehydrogenase (CoA-acylating)Advanced search results
results (
results (Engineering
Engineering on EC 1.2.1.27 - methylmalonate-semialdehyde dehydrogenase (CoA-acylating)
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
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
V229G/H226P
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
additional information
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
Pyricularia oryzae ATCC MYA-4617
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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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additional information
Pyricularia oryzae FGSC 8958
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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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