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EC Tree
IUBMB 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).
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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(+)-citramalate pyruvate-lyase
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(S)-citramalate lyase
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citramalate synthetase
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citramalic synthase
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citramalic-condensing enzyme
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lyase, citramalate
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CimA
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citramalate lyase
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citramalate synthase
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citramalate synthase
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citramalate synthase
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GSU1798
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represents a novel phylogenetic variant of the enzyme
GSU1798
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represents a novel phylogenetic variant of the enzyme
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GSU1798
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represents a novel phylogenetic variant of the enzyme
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(2S)-2-hydroxy-2-methylbutanedioate = acetate + pyruvate
(2S)-2-hydroxy-2-methylbutanedioate = acetate + pyruvate
reversible nucleophilic addition of acetyl thioester to carbonyl groups with inversion of congfiguration
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(2S)-2-hydroxy-2-methylbutanedioate = acetate + pyruvate
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elimination
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of an oxo-acid, C-C bond cleavage
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(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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acetate + pyruvate
(+)-citramalate
acetate + pyruvate
citramalate
citramalate
2-oxobutanoate + ?
citramalate
acetate + pyruvate
additional information
?
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the enzyme is involved in the fermentation of glutamate
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?
acetate + pyruvate
(+)-citramalate
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?
acetate + pyruvate
(+)-citramalate
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?
acetate + pyruvate
(+)-citramalate
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?
acetate + pyruvate
(+)-citramalate
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?
acetate + pyruvate
(+)-citramalate
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enzyme of the citramalate cycle, acetate assimilation involves the operation of the citramalate cycle
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?
acetate + pyruvate
(+)-citramalate
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?
acetate + pyruvate
citramalate
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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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?
acetate + pyruvate
citramalate
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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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?
acetate + pyruvate
citramalate
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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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?
acetate + pyruvate
citramalate
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?
acetate + pyruvate
citramalate
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?
acetate + pyruvate
citramalate
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?
acetate + pyruvate
citramalate
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?
citramalate
2-oxobutanoate + ?
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?
citramalate
2-oxobutanoate + ?
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?
citramalate
2-oxobutanoate + ?
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?
citramalate
acetate + pyruvate
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?
citramalate
acetate + pyruvate
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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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?
citramalate
acetate + pyruvate
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(+)-citramalate
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?
citramalate
acetate + pyruvate
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?
citramalate
acetate + pyruvate
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?
citramalate
acetate + pyruvate
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?
citramalate
acetate + pyruvate
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?
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acetate + pyruvate
(+)-citramalate
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enzyme of the citramalate cycle, acetate assimilation involves the operation of the citramalate cycle
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?
acetate + pyruvate
citramalate
additional information
?
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the enzyme is involved in the fermentation of glutamate
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?
acetate + pyruvate
citramalate
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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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?
acetate + pyruvate
citramalate
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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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?
acetate + pyruvate
citramalate
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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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?
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Co2+
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Mn2+, Mg2+ or Co2+ required
Mn2+
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Mn2+, Mg2+ or Co2+ required
Mg2+
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or an equivalent divalent cation is required
Mg2+
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Km for MgCl2: 0.1 mM
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dephospho-CoA
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bound in phosphodiester linkage to Ser and glycosidically to the 2' or 3'-hydroxyl group of ribose of dephospho-CoA
additional information
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the enzyme contains acetyl thioester residues which play the central role in the catalytic mechanism
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Leptospirosis
Molecular basis of the inhibitor selectivity and insights into the feedback inhibition mechanism of citramalate synthase from Leptospira interrogans.
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33.14
in TES buffer (0.1 M, pH 7.5), at 37°C
37.43
in TES buffer (0.1 M, pH 7.5), at 37°C
39.42
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
80.92
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
0.0004
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in mutant strain DLCR6 (cimA::Gm)
0.0004
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in mutant strain DLCR7 (tdcB::Kn cimA::Gm)
additional information
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additional information
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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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7.3 - 7.5
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50 mM potassium phosphate buffer
8 - 8.2
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Tris-HCl buffer
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6 - 8
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pH 6.0: 52% of maximal activity, pH 8.0: 77% of maximal activity, in 50 mM potassium phosphate buffer
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brenda
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brenda
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brenda
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brenda
fragment; serovar Semaranga
SwissProt
brenda
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brenda
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brenda
no activity in Clostridium kluyveri
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brenda
no activity in Escherichia coli
ATCC 4157
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brenda
no activity in Pseudomonas sp.
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brenda
no activity in Saccharomyces cerevisiae
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brenda
fragment; serovar Monteralerio
SwissProt
brenda
fragment; serovar Patoc I
SwissProt
brenda
fragment; serovar Australis
SwissProt
brenda
fragment; serovar Autumnalis
SwissProt
brenda
fragment; serovar Canicola
SwissProt
brenda
fragment; serovar Hebdomadis
SwissProt
brenda
fragment; serovar Lai
SwissProt
brenda
fragment; serovar Pomona
SwissProt
brenda
fragment; serovar Pyrogenes
SwissProt
brenda
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A0FDH8_LEPIR
426
0
47186
TrEMBL
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A0FDI0_LEPIR
435
0
48217
TrEMBL
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A0FDI2_LEPIR
431
0
47831
TrEMBL
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A0FDI4_LEPIR
434
0
48195
TrEMBL
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A0FDI6_LEPIR
427
0
47296
TrEMBL
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A0FDI8_LEPIR
435
0
48217
TrEMBL
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A0FDJ0_LEPIR
435
0
48159
TrEMBL
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A0FDJ2_LEPBI
437
0
48568
TrEMBL
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A0FDJ4_LEPBI
431
0
47955
TrEMBL
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A1Z0Z6_LEPME
435
0
48388
TrEMBL
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520000 - 580000
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gel filtration, sucrose density gradient centrifugation
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oligomer
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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
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6 * 53000-56000, alpha, + 6 * 33000-36000, beta, + 6 * 10000-12000, gamma, SDS-PAGE
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DLCR6 (cimA::Gm)
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citramalate synthase knockout mutant
DLCR7 (tdcB::Kn cimA::Gm)
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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)
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citramalate synthase knockout mutant
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DLCR7 (tdcB::Kn cimA::Gm)
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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
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DLCR6 (cimA::Gm)
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citramalate synthase knockout mutant
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DLCR7 (tdcB::Kn cimA::Gm)
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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
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additional information
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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
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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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additional information
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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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-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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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
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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
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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
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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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