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Information on EC 4.1.3.22 - citramalate lyase
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4.1.3.22 citramalate lyaseIUBMB Comments
The enzyme can be dissociated into components, two of which are identical with EC 2.8.3.11 (citramalate CoA-transferase) and EC 4.1.3.25 (citramalyl-CoA lyase).
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Word Map
- 4.1.3.22
- isoleucine
- jannaschii
-
methanococcus
- interrogans
- leptospira
-
five-carbon
- tetanomorphum
- 2-isopropylmalate
- 1-propanol
- citraconate
-
isotopomer
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
(+)-citramalate pyruvate-lyase, (S)-citramalate lyase, CimA, citramalate lyase, citramalate synthase, citramalate synthetase, citramalic synthase, citramalic-condensing enzyme, CMS, GSU1798, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
(+)-citramalate pyruvate-lyase
-
-
-
-
(S)-citramalate lyase
-
-
-
-
CimA
citramalate lyase
citramalate synthase
citramalate synthetase
-
-
-
-
citramalic synthase
-
-
-
-
citramalic-condensing enzyme
-
-
-
-
GSU1798
lyase, citramalate
-
-
-
-
citramalate lyase
-
citramalate synthase
-
-
-
-
GSU1798
Geobacter sulfurreducens ATCC 51573 / DSM 12127
-
represents a novel phylogenetic variant of the enzyme
-
GSU1798
-
represents a novel phylogenetic variant of the enzyme
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(2S)-2-hydroxy-2-methylbutanedioate = acetate + pyruvate
reversible nucleophilic addition of acetyl thioester to carbonyl groups with inversion of congfiguration
-
(2S)-2-hydroxy-2-methylbutanedioate = acetate + pyruvate
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
condensation
-
-
-
-
elimination
-
-
of an oxo-acid, C-C bond cleavage
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
(2S)-2-hydroxy-2-methylbutanedioate pyruvate-lyase (acetate-forming)
The enzyme can be dissociated into components, two of which are identical with EC 2.8.3.11 (citramalate CoA-transferase) and EC 4.1.3.25 (citramalyl-CoA lyase).
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CAS REGISTRY NUMBER
COMMENTARY
9027-93-4
-
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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
additional information
?
-
-
the enzyme is involved in the fermentation of glutamate
-
-
?
acetate + pyruvate
(+)-citramalate
-
enzyme of the citramalate cycle, acetate assimilation involves the operation of the citramalate cycle
-
-
?
acetate + pyruvate
citramalate
-
citramalate synthase appears to have a high affinity for pyruvate, with 52.5% +/- 4.9% of the activity remaining when the pyruvate concentration is reduced from 1 mM to 0.1 mM
-
-
?
acetate + pyruvate
citramalate
Geobacter sulfurreducens ATCC 51573 / DSM 12127
-
citramalate synthase appears to have a high affinity for pyruvate, with 52.5% +/- 4.9% of the activity remaining when the pyruvate concentration is reduced from 1 mM to 0.1 mM
-
-
?
acetate + pyruvate
citramalate
-
citramalate synthase appears to have a high affinity for pyruvate, with 52.5% +/- 4.9% of the activity remaining when the pyruvate concentration is reduced from 1 mM to 0.1 mM
-
-
?
acetate + pyruvate
citramalate
-
-
-
?
citramalate
acetate + pyruvate
-
the alpha-subunit catalyzes the formation of acetyl-CoA and citramalate. The beta-subunit catalyzes the cleavage of (3S)-citramalyl-thio-acyl carrier protein lyase
-
?
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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
acetate + pyruvate
(+)-citramalate
-
enzyme of the citramalate cycle, acetate assimilation involves the operation of the citramalate cycle
-
-
?
additional information
?
-
-
the enzyme is involved in the fermentation of glutamate
-
-
?
acetate + pyruvate
citramalate
-
citramalate synthase appears to have a high affinity for pyruvate, with 52.5% +/- 4.9% of the activity remaining when the pyruvate concentration is reduced from 1 mM to 0.1 mM
-
-
?
acetate + pyruvate
citramalate
Geobacter sulfurreducens ATCC 51573 / DSM 12127
-
citramalate synthase appears to have a high affinity for pyruvate, with 52.5% +/- 4.9% of the activity remaining when the pyruvate concentration is reduced from 1 mM to 0.1 mM
-
-
?
acetate + pyruvate
citramalate
-
citramalate synthase appears to have a high affinity for pyruvate, with 52.5% +/- 4.9% of the activity remaining when the pyruvate concentration is reduced from 1 mM to 0.1 mM
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
dephospho-CoA
-
bound in phosphodiester linkage to Ser and glycosidically to the 2' or 3'-hydroxyl group of ribose of dephospho-CoA
additional information
-
the enzyme contains acetyl thioester residues which play the central role in the catalytic mechanism
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Leptospirosis
Molecular basis of the inhibitor selectivity and insights into the feedback inhibition mechanism of citramalate synthase from Leptospira interrogans.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0004
37.43
in TES buffer (0.1 M, pH 7.5), at 37°C
44.35
in TES buffer (0.1 M, pH 7.5), at 37°C
51.29
in TES buffer (0.1 M, pH 7.5), at 37°C
53.68
in TES buffer (0.1 M, pH 7.5), at 37°C
64.75
in TES buffer (0.1 M, pH 7.5), at 37°C
76.46
in TES buffer (0.1 M, pH 7.5), at 37°C
82.36
in TES buffer (0.1 M, pH 7.5), at 37°C
additional information
additional information
-
enzymatic activity in mutant strain DLCR5 (tdcB::Kn), a threonine ammonia-lyase knockout mutant (EC 4.3.1.19), is 0.0051 micromol/min/mg
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 8
-
pH 6.0: 52% of maximal activity, pH 8.0: 77% of maximal activity, in 50 mM potassium phosphate buffer
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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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). A0FDI0_LEPIR
435
0
48217
TrEMBL
-
A0FDI2_LEPIR
431
0
47831
TrEMBL
-
A0FDI4_LEPIR
434
0
48195
TrEMBL
-
A0FDI6_LEPIR
427
0
47296
TrEMBL
-
A0FDJ0_LEPIR
435
0
48159
TrEMBL
-
A0FDJ2_LEPBI
437
0
48568
TrEMBL
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
520000 - 580000
-
gel filtration, sucrose density gradient centrifugation
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oligomer
oligomer
-
the alpha-subunit represents an acetyl-thio-acyl carrier protein:citramalate acyl carrier protein transferase and the beta-subunit a (3S)-citramalyl-thio-acyl carrier protein lyase
oligomer
-
6 * 53000-56000, alpha, + 6 * 33000-36000, beta, + 6 * 10000-12000, gamma, SDS-PAGE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
DLCR7 (tdcB::Kn cimA::Gm)
-
double (ammonia-lyase (EC 4.3.1.19) and citramalate synthase) knockout mutant. DLCR5 (tdcB::Kn) a threonine ammonia-lyase knockout mutant (EC 4.3.1.19) is also constructed
DLCR6 (cimA::Gm)
Geobacter sulfurreducens ATCC 51573 / DSM 12127
-
citramalate synthase knockout mutant
-
DLCR7 (tdcB::Kn cimA::Gm)
Geobacter sulfurreducens ATCC 51573 / DSM 12127
-
double (ammonia-lyase (EC 4.3.1.19) and citramalate synthase) knockout mutant. DLCR5 (tdcB::Kn) a threonine ammonia-lyase knockout mutant (EC 4.3.1.19) is also constructed
-
DLCR7 (tdcB::Kn cimA::Gm)
-
double (ammonia-lyase (EC 4.3.1.19) and citramalate synthase) knockout mutant. DLCR5 (tdcB::Kn) a threonine ammonia-lyase knockout mutant (EC 4.3.1.19) is also constructed
-
additional information
additional information
-
strain DL1 used to construct strains. Construction of mutants via single-step gene replacement. Mutants lacking both enzymes (citramalate synthase and threonine ammonia-lyase) are auxotrophs for isoleucine, whereas single mutants are capable of growth in the absence of isoleucine
additional information
Geobacter sulfurreducens ATCC 51573 / DSM 12127
-
strain DL1 used to construct strains. Construction of mutants via single-step gene replacement. Mutants lacking both enzymes (citramalate synthase and threonine ammonia-lyase) are auxotrophs for isoleucine, whereas single mutants are capable of growth in the absence of isoleucine
-
additional information
-
strain DL1 used to construct strains. Construction of mutants via single-step gene replacement. Mutants lacking both enzymes (citramalate synthase and threonine ammonia-lyase) are auxotrophs for isoleucine, whereas single mutants are capable of growth in the absence of isoleucine
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, enzyme concentration 10 mg/ml, 0.1 M phoshate, pH 7.4, 1.0 mM MgCl2, stable for at least 6 months
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Barker, H.A.
Citramalate lyase of Clostridium tetanomorphum
Arch. Mikrobiol.
59
4-12
1967
Clostridium tetanomorphum, Clostridium tetanomorphum H1 / ATCC 15920, no activity in Clostridium kluyveri, no activity in Escherichia coli, no activity in Pseudomonas sp., no activity in Saccharomyces cerevisiae
brenda
Barker, H.A.
Citramalate pyruvate lyase
Methods Enzymol.
13
344-346
1969
Clostridium tetanomorphum
-
brenda
Buckel, W.; Bobi, A.
The enzyme complex citramalate lyase from Clostridium tetanomorphum
Eur. J. Biochem.
64
255-262
1976
Clostridium tetanomorphum
brenda
Dimroth, P.; Buckel, W.; Loyal, R.; Eggerer, H.
Isolation and function of the subunits of citramalate lyase and formation of hybrids with the subunits of citrate lyase
Eur. J. Biochem.
80
469-477
1977
Clostridium tetanomorphum
brenda
Dimroth, P.; Loyal, R.
Structure of the prosthetic groups of citrate lyase and citramalate lyase
FEBS Lett.
76
280-283
1977
Clostridium tetanomorphum
brenda
Buckel, W.; Bobi, A.
Substrate stereochemistry of the cleavage reaction in citramalate lyase
Biochem. Soc. Trans.
3
924-926
1975
Clostridium tetanomorphum
-
brenda
Filatova, L.V.; Berg, I.A.; Krasil'nikova, E.N.; Ivanovsky, R.N.
A study of the mechanism of acetate assimilation in purple nonsulfur bacteria lacking the glyoxylate shunt: enzymes of the citramalate cycle in Rhodobacter sphaeroides
Microbiology
74
270-278
2005
Luteovulum sphaeroides
-
brenda
Zou, Y.; Guo, X.; Picardeau, M.; Xu, H.; Zhao, G.
A comprehensive survey on isoleucine biosynthesis pathways in seven epidemic Leptospira interrogans reference strains of China
FEMS Microbiol. Lett.
269
90-96
2007
Leptospira biflexa (A0FDJ2), Leptospira biflexa (A0FDJ4), Leptospira biflexa, Leptospira interrogans (A0FDH8), Leptospira interrogans (A0FDI0), Leptospira interrogans (A0FDI2), Leptospira interrogans (A0FDI4), Leptospira interrogans (A0FDI6), Leptospira interrogans (A0FDI8), Leptospira interrogans (A0FDJ0), Leptospira interrogans, Leptospira meyeri (A1Z0Z6), Leptospira meyeri
brenda
Drevland, R.M.; Waheed, A.; Graham, D.E.
Enzymology and evolution of the pyruvate pathway to 2-oxobutyrate in Methanocaldococcus jannaschii
J. Bacteriol.
189
4391-4400
2007
Methanocaldococcus jannaschii
brenda
Risso, C.; Van Dien, S.J.; Orloff, A.; Lovley, D.R.; Coppi, M.V.
Elucidation of an alternate isoleucine biosynthesis pathway in Geobacter sulfurreducens
J. Bacteriol.
190
2266-2274
2008
Geobacter sulfurreducens, Geobacter sulfurreducens ATCC 51573 / DSM 12127
brenda
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