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Information on EC 2.3.3.18 - 2-phosphinomethylmalate synthase
for references in articles please use BRENDA:EC2.3.3.18
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EC Tree 2 Transferases
2.3 Acyltransferases
2.3.3 Acyl groups converted into alkyl groups on transfer
2.3.3.18 2-phosphinomethylmalate synthase
IUBMB Comments
The enzyme, characterized from the bacterium Streptomyces hygroscopicus, participates in the pathway for bialaphos biosynthesis. It requires a divalent metal ion and can also act on oxaloacetate.
The expected taxonomic range for this enzyme is: Streptomyces hygroscopicus
Reaction Schemes
showSynonyms
2-phosphinomethylmalate synthase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2-phosphinomethylmalic acid synthase
pmmS
pmmS
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
acetyl-CoA + H2O + 3-(hydroxyphosphinoyl)pyruvate = phosphinomethylmalate + CoA
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
phosalacine biosynthesis, phosphinothricin tripeptide biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:phosphinopyruvate C-acetyltransferase (thioester-hydrolysing, phosphinomethylmalate-forming)
The enzyme, characterized from the bacterium Streptomyces hygroscopicus, participates in the pathway for bialaphos biosynthesis. It requires a divalent metal ion and can also act on oxaloacetate.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + H2O + oxaloacetate
?
Substrates: the enzyme uses an active-site architecture similar to homocitrate synthase to select for a dicarboxylic acid substrate
Products: -
Products: -
?
acetyl-CoA + H2O + 3-(hydroxyphosphinoyl)pyruvate
phosphinomethylmalate + CoA
Substrates: -
Products: -
Products: -
?
acetyl-CoA + H2O + 3-(hydroxyphosphinoyl)pyruvate
phosphinomethylmalate + CoA
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + H2O + 3-(hydroxyphosphinoyl)pyruvate
phosphinomethylmalate + CoA
Substrates: -
Products: -
Products: -
?
acetyl-CoA + H2O + 3-(hydroxyphosphinoyl)pyruvate
phosphinomethylmalate + CoA
Substrates: -
Products: -
Products: -
?
acetyl-CoA + H2O + oxaloacetic acid
? + CoA
Substrates: -
Products: -
Products: -
?
acetyl-CoA + H2O + oxaloacetic acid
? + CoA
Substrates: -
Products: -
Products: -
?
additional information
?
-
Substrates: no substrates: propionyl-CoA or butanoyl-CoA and alpha-oxoacids such as pyruvate, 2-oxoglutarate, deamino-2-oxodemethylphosphinotricin or phosphonopyruvate
Products: -
Products: -
?
additional information
?
-
-
Substrates: no substrates: propionyl-CoA or butanoyl-CoA and alpha-oxoacids such as pyruvate, 2-oxoglutarate, deamino-2-oxodemethylphosphinotricin or phosphonopyruvate
Products: -
Products: -
?
additional information
?
-
Substrates: no substrates: propionyl-CoA or butanoyl-CoA and alpha-oxoacids such as pyruvate, 2-oxoglutarate, deamino-2-oxodemethylphosphinotricin or phosphonopyruvate
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + H2O + 3-(hydroxyphosphinoyl)pyruvate
phosphinomethylmalate + CoA
Substrates: -
Products: -
Products: -
?
acetyl-CoA + H2O + 3-(hydroxyphosphinoyl)pyruvate
phosphinomethylmalate + CoA
Substrates: -
Products: -
Products: -
?
acetyl-CoA + H2O + oxaloacetic acid
? + CoA
Substrates: -
Products: -
Products: -
?
acetyl-CoA + H2O + oxaloacetic acid
? + CoA
Substrates: -
Products: -
Products: -
?
additional information
?
-
Substrates: no substrates: propionyl-CoA or butanoyl-CoA and alpha-oxoacids such as pyruvate, 2-oxoglutarate, deamino-2-oxodemethylphosphinotricin or phosphonopyruvate
Products: -
Products: -
?
additional information
?
-
-
Substrates: no substrates: propionyl-CoA or butanoyl-CoA and alpha-oxoacids such as pyruvate, 2-oxoglutarate, deamino-2-oxodemethylphosphinotricin or phosphonopyruvate
Products: -
Products: -
?
additional information
?
-
Substrates: no substrates: propionyl-CoA or butanoyl-CoA and alpha-oxoacids such as pyruvate, 2-oxoglutarate, deamino-2-oxodemethylphosphinotricin or phosphonopyruvate
Products: -
Products: -
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
MnCl2
addition of MnCl2 up to 1 mM results in a two-fold stimulation of activity but greater concentrations result in decreased activity
additional information
the enzyme is active in the absence of exogenous divalent metal ions and addition of 1 mM EDTA
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
phosphate buffer
not inhibitory at 10 mM, 50% loss of activity in 100 mM phosphate buffer
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.003
acetyl-CoA
pH 7.8, 25°C, mutant enzyme R173A, apparent KM value from Michaelis-Menten plots due to inability to accurately measure activity at substrate concentrations less than 0.0025 mM
0.004
acetyl-CoA
pH 7.8, 25°C, mutant enzyme E82Q, apparent KM value from Michaelis-Menten plots due to inability to accurately measure activity at substrate concentrations less than 0.0025 mM
0.006
acetyl-CoA
pH 7.8, 25°C, mutant enzyme E82A, apparent KM value from Michaelis-Menten plots due to inability to accurately measure activity at substrate concentrations less than 0.0025 mM
0.004
oxaloacetate
pH 7.8, 25°C, mutant enzyme E82Q, apparent KM value from Michaelis-Menten plots due to inability to accurately measure activity at substrate concentrations less than 0.0025 mM
0.004
oxaloacetate
pH 7.8, 25°C, mutant enzyme W112A, apparent KM value from Michaelis-Menten plots due to inability to accurately measure activity at substrate concentrations less than 0.0025 mM
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
the enzyme catalyzes the first step in the biosynthesis of the herbicide bialophos
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, lyophilized powder, 5% loss of activity within 3 months
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Shimotohno, K.; Seto, H.; Imai, S.; Murakami, T.
Purification and characterization of citrate synthase from Streptomyces hygroscopicus SF-1293 and comparison of its properties with those of 2-phosphinomethylmalic acid synthase
Agric. Biol. Chem.
54
463-470
1990
Streptomyces hygroscopicus (Q9LCB4), Streptomyces hygroscopicus, Streptomyces hygroscopicus SF-1293 (Q9LCB4)
brenda
Shimotohno, K.; Seto, H.; Ōtake, N.; Imai, S.; Murakami, T.
Studies on the biosynthesis of bialaphos (SF-1293). 8. Purification and characterization of 2-phosphinomethylmalic acid synthase from Streptomyces hygroscopicus SF-1293
J. Antibiot.
41
1057-1065
1988
Streptomyces hygroscopicus (Q9LCB4), Streptomyces hygroscopicus, Streptomyces hygroscopicus SF-1293 (Q9LCB4)
brenda
Conte, J.V.; Frantom, P.A.
Biochemical characterization of 2-phosphinomethylmalate synthase from Streptomyces hygroscopicus A member of the DRE-TIM metallolyase superfamily
Arch. Biochem. Biophys.
691
108489
2020
Streptomyces hygroscopicus (Q9LCB4)
brenda
EXTERNAL LINKS (specific for EC-Number 2.3.3.18)
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