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Information on EC 4.2.1.114 - methanogen homoaconitase
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4.2.1.114 methanogen homoaconitaseIUBMB Comments
This enzyme catalyses several reactions in the pathway of coenzyme-B biosynthesis in methanogenic archaea. Requires a [4Fe-4S] cluster for activity. In contrast to EC 4.2.1.36, homoaconitate hydratase, this enzyme can catalyse both the dehydration of (R)-homocitrate to form cis-homoaconitate and the subsequent hydration reaction that forms homoisocitrate. In addition to cis-homoaconitate, the enzyme can also catalyse the hydration of the physiological substrates dihomoaconitate and trihomoaconitate as well as the non-physiological substrate tetrahomoaconitate. cis-Aconitate and threo-DL-isocitrate cannot act as substrates, and (S)-homocitrate and trans-homoaconitate act as inhibitors of the enzyme.
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The expected taxonomic range for this enzyme is: Archaea, Bacteria
Reaction Schemes
Synonyms
mj1003, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CNAG_02565
HacA
HACN
Homoaconitase
LYS4
methanogen HACN
-
-
-
-
MJ1003
additional information
the enzyme belongs to the aconitase superfamily
CNAG_02565
Cryptococcus neoformans var. grubii serotype A H99 / ATCC 208821 / CBS 10515 / FGSC 9487
-
-
Homoaconitase
Cryptococcus neoformans var. grubii serotype A H99 / ATCC 208821 / CBS 10515 / FGSC 9487
-
-
LYS4
Cryptococcus neoformans var. grubii serotype A H99 / ATCC 208821 / CBS 10515 / FGSC 9487
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(R)-2-hydroxybutane-1,2,4-tricarboxylate = (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate
overall reaction
-
-
-
(R)-2-hydroxybutane-1,2,4-tricarboxylate = (Z)-but-1-ene-1,2,4-tricarboxylate + H2O
-
-
-
-
(Z)-but-1-ene-1,2,4-tricarboxylate + H2O = (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
(R)-2-hydroxybutane-1,2,4-tricarboxylate hydro-lyase [(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate-forming]
This enzyme catalyses several reactions in the pathway of coenzyme-B biosynthesis in methanogenic archaea. Requires a [4Fe-4S] cluster for activity. In contrast to EC 4.2.1.36, homoaconitate hydratase, this enzyme can catalyse both the dehydration of (R)-homocitrate to form cis-homoaconitate and the subsequent hydration reaction that forms homoisocitrate. In addition to cis-homoaconitate, the enzyme can also catalyse the hydration of the physiological substrates dihomoaconitate and trihomoaconitate as well as the non-physiological substrate tetrahomoaconitate. cis-Aconitate and threo-DL-isocitrate cannot act as substrates, and (S)-homocitrate and trans-homoaconitate act as inhibitors of the enzyme.
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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
(1E)-hex-1-ene-1,2,6-tricarboxylic acid + H2O
(2R)-hexane-1,2,6-tricarboxyclic acid
-
-
-
-
?
(1E)-pent-1-ene-1,2,5-tricarboxylic acid + H2O
(2R)-pentane-1,2,5-tricarboxylic acid
-
-
-
-
?
(2R)-butane-1,2,4-tricarboxylic acid
but-1-ene-1,2,4-tricarboxylic acid + H2O
-
-
-
-
?
(R)-2-hydroxybutane-1,2,4-tricarboxylate
(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate
i.e. (R)-homocitrate, overall reaction, the enzyme catalyzes both the dehydration of (R)-homocitrate to form cis-homoaconitate, and hydration producing homoisocitrate
i.e. homoisocitrate
-
r
(R)-2-hydroxybutane-1,2,4-tricarboxylate + H2O
(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate
but-1-ene-1,2,4-tricarboxylic acid + H2O
(2R)-butane-1,2,4-tricarboxylic acid
-
-
-
-
?
cis-(homo)2aconitate + H2O
(-)-threo-iso(homo)2citrate
-
-
-
?
cis-(homo)2aconitate + H2O
?
the activity is similar as with (R)-homocitrate
-
-
?
cis-(homo)3aconitate + H2O
(-)-threo-iso(homo)3citrate
-
-
-
?
cis-(homo)3aconitate + H2O
?
the activity is similar as with (R)-homocitrate
-
-
?
cis-(homo)4aconitate + H2O
?
the activity is similar as with (R)-homocitrate
-
-
?
(R)-2-hydroxybutane-1,2,4-tricarboxylate
(Z)-but-1-ene-1,2,4-tricarboxylate + H2O
Cryptococcus neoformans var. grubii serotype A
-
-
-
?
(R)-2-hydroxybutane-1,2,4-tricarboxylate
(Z)-but-1-ene-1,2,4-tricarboxylate + H2O
Cryptococcus neoformans var. grubii serotype A H99 / ATCC 208821 / CBS 10515 / FGSC 9487
-
-
-
?
(R)-2-hydroxybutane-1,2,4-tricarboxylate
(Z)-but-1-ene-1,2,4-tricarboxylate + H2O
i.e. (R)-homocitrate, first half-reaction
i.e. cis-homoaconitate, the activity in the reverse direction is similar as with (R)-homocitrate
-
r
(R)-2-hydroxybutane-1,2,4-tricarboxylate + H2O
(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate
Cryptococcus neoformans var. grubii serotype A
-
-
-
?
(R)-2-hydroxybutane-1,2,4-tricarboxylate + H2O
(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate
Cryptococcus neoformans var. grubii serotype A H99 / ATCC 208821 / CBS 10515 / FGSC 9487
-
-
-
?
(Z)-but-1-ene-1,2,4-tricarboxylate + H2O
(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate
Cryptococcus neoformans var. grubii serotype A
-
-
-
?
(Z)-but-1-ene-1,2,4-tricarboxylate + H2O
(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate
Cryptococcus neoformans var. grubii serotype A H99 / ATCC 208821 / CBS 10515 / FGSC 9487
-
-
-
?
(Z)-but-1-ene-1,2,4-tricarboxylate + H2O
(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate
second half-reaction
i.e. homoisocitrate
-
r
additional information
?
-
-
homoaconitase enzymes catalyze hydrolyase reactions in the alpha-aminoadipate pathway for lysine biosynthesis or the 2-oxosuberate pathway for methanogenic coenzyme B biosynthesis
-
-
?
additional information
?
-
homoaconitase enzymes catalyze hydrolyase reactions in the alpha-aminoadipate pathway for lysine biosynthesis or the 2-oxosuberate pathway for methanogenic coenzyme B biosynthesis
-
-
?
additional information
?
-
-
homoaconitase together with the endogenous homoisocitrate dehydrogenase, EC 1.1.1.87, catalyze all of the isomerization and oxidative decarboxylation reactions required to form 2-oxoadipate, 2-oxopimelate, and 2-oxosuberate, completing three iterations of the 2-oxoacid elongation pathway. Methanogenic archaeal homoaconitases and fungal homoaconitases evolved in parallel in the aconitase superfamily, LC-MS analysis of enzyme reaction products, overview
-
-
?
additional information
?
-
homoaconitase together with the endogenous homoisocitrate dehydrogenase, EC 1.1.1.87, catalyze all of the isomerization and oxidative decarboxylation reactions required to form 2-oxoadipate, 2-oxopimelate, and 2-oxosuberate, completing three iterations of the 2-oxoacid elongation pathway. Methanogenic archaeal homoaconitases and fungal homoaconitases evolved in parallel in the aconitase superfamily, LC-MS analysis of enzyme reaction products, overview
-
-
?
additional information
?
-
-
HACN has no detectable activity with citraconate or isopropylmalate
-
-
?
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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
(R)-2-hydroxybutane-1,2,4-tricarboxylate + H2O
(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate
cis-(homo)2aconitate + H2O
(-)-threo-iso(homo)2citrate
-
-
-
?
cis-(homo)3aconitate + H2O
(-)-threo-iso(homo)3citrate
-
-
-
?
(R)-2-hydroxybutane-1,2,4-tricarboxylate
(Z)-but-1-ene-1,2,4-tricarboxylate + H2O
Cryptococcus neoformans var. grubii serotype A
-
-
-
?
(R)-2-hydroxybutane-1,2,4-tricarboxylate
(Z)-but-1-ene-1,2,4-tricarboxylate + H2O
Cryptococcus neoformans var. grubii serotype A H99 / ATCC 208821 / CBS 10515 / FGSC 9487
-
-
-
?
(R)-2-hydroxybutane-1,2,4-tricarboxylate + H2O
(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate
Cryptococcus neoformans var. grubii serotype A
-
-
-
?
(R)-2-hydroxybutane-1,2,4-tricarboxylate + H2O
(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate
Cryptococcus neoformans var. grubii serotype A H99 / ATCC 208821 / CBS 10515 / FGSC 9487
-
-
-
?
(Z)-but-1-ene-1,2,4-tricarboxylate + H2O
(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate
Cryptococcus neoformans var. grubii serotype A
-
-
-
?
(Z)-but-1-ene-1,2,4-tricarboxylate + H2O
(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate
Cryptococcus neoformans var. grubii serotype A H99 / ATCC 208821 / CBS 10515 / FGSC 9487
-
-
-
?
additional information
?
-
-
homoaconitase enzymes catalyze hydrolyase reactions in the alpha-aminoadipate pathway for lysine biosynthesis or the 2-oxosuberate pathway for methanogenic coenzyme B biosynthesis
-
-
?
additional information
?
-
homoaconitase enzymes catalyze hydrolyase reactions in the alpha-aminoadipate pathway for lysine biosynthesis or the 2-oxosuberate pathway for methanogenic coenzyme B biosynthesis
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
Iron-sulfur cluster
the structure of the protein has unbound Fe-S clusters and contains a fourth cysteine in the active site
Mg2+
required for the hydratase reaction, not for the hydrolase reaction
Fe2+
the enzyme contains an iron-sulfur center, reconstitution of the purified recombinant apoenzyme with iron-sulfur, overview
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
cis-aconitate
50% inhibition of the hydrolase activity at 0.025 mM
cis-homoaconitate/(R)-homocitrate
mixtures of 0.1 mM cis-homoaconitate and 0.05 mM (R)-homocitrate reduce the HACN hydrolyase activity by 50%
trans-(homo)3aconitate
50% inhibition of the hydrolase activity at 0.4 mM
trans-aconitate
50% inhibition of the hydrolase activity at 0.1 mM
additional information
-
no inhibition by citraconate up to 0.2 mM
-
additional information
no inhibition by citraconate up to 0.2 mM
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Dehydration
Methanogen homoaconitase catalyzes both hydrolyase reactions in coenzyme B biosynthesis.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.5
(R)-homocitrate
pH 8.5, 60°C, recombinant enzyme, dehydratase reaction
0.03
cis-homo2aconitate
pH 9.0, 60°C, recombinant enzyme, hydrolase reaction
0.036
cis-homo3aconitate
pH 9.0, 60°C, recombinant enzyme, hydrolase reaction
0.175
cis-homo4aconitate
pH 9.0, 60°C, recombinant enzyme, hydrolase reaction
0.022
cis-homoaconitate
pH 9.0, 60°C, recombinant enzyme, hydrolase reaction
0.33
Maleate
pH 9.0, 60°C, recombinant enzyme, hydrolase reaction
0.036
(1E)-hex-1-ene-1,2,6-tricarboxylic acid
-
wild type enzyme
0.64
(1E)-hex-1-ene-1,2,6-tricarboxylic acid
-
mutant enzyme R26V/T27Y
0.65
(1E)-hex-1-ene-1,2,6-tricarboxylic acid
-
mutant enzyme T27A
0.66
(1E)-hex-1-ene-1,2,6-tricarboxylic acid
-
mutant enzyme R26V
0.03
(1E)-pent-1-ene-1,2,5-tricarboxylic acid
-
wild type enzyme
0.269
(1E)-pent-1-ene-1,2,5-tricarboxylic acid
-
mutant enzyme T27A
0.87
(1E)-pent-1-ene-1,2,5-tricarboxylic acid
-
mutant enzyme R26V
1.6
(1E)-pent-1-ene-1,2,5-tricarboxylic acid
-
mutant enzyme R26V/T27Y
0.46
but-1-ene-1,2,4-tricarboxylic acid
-
mutant enzyme R26V/T27Y
additional information
additional information
-
steady-state kinetics
-
additional information
additional information
steady-state kinetics
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.37
(R)-homocitrate
pH 8.5, 60°C, recombinant enzyme, dehydratase reaction
0.66
cis-homo2aconitate
pH 9.0, 60°C, recombinant enzyme, hydrolase reaction
2.5
cis-homo3aconitate
pH 9.0, 60°C, recombinant enzyme, hydrolase reaction
5.6
cis-homo4aconitate
pH 9.0, 60°C, recombinant enzyme, hydrolase reaction
0.75
cis-homoaconitate
pH 9.0, 60°C, recombinant enzyme, hydrolase reaction
6
Maleate
pH 9.0, 60°C, recombinant enzyme, hydrolase reaction
1.9
(1E)-hex-1-ene-1,2,6-tricarboxylic acid
-
mutant enzyme R26V/T27Y
2.8
(1E)-hex-1-ene-1,2,6-tricarboxylic acid
-
mutant enzyme R26V
4.1
(1E)-hex-1-ene-1,2,6-tricarboxylic acid
-
mutant enzyme T27A
0.66
(1E)-pent-1-ene-1,2,5-tricarboxylic acid
-
wild type enzyme
2.2
(1E)-pent-1-ene-1,2,5-tricarboxylic acid
-
mutant enzyme T27A
5.8
(1E)-pent-1-ene-1,2,5-tricarboxylic acid
-
mutant enzyme R26V
6.6
(1E)-pent-1-ene-1,2,5-tricarboxylic acid
-
mutant enzyme R26V/T27Y
1.7
but-1-ene-1,2,4-tricarboxylic acid
-
mutant enzyme R26V/T27Y
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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
Cryptococcus neoformans var. grubii serotype A H99 / ATCC 208821 / CBS 10515 / FGSC 9487
-
UniProt
brenda
large subunit of homoaconitase
SwissProt
brenda
the sequence contains the alteration C229A resulting in Q77K amino acid exchange compared to the MJ1596 sequence reported by the genome sequencing project, cf. EC 1.1.1.87; proteins MJ1003 and MJ1271
UniProt
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Cryptococcus neoformans var. grubii serotype A H99 / ATCC 208821 / CBS 10515 / FGSC 9487
-
-
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
malfunction
Cryptococcus neoformans var. grubii serotype A
deletion of the CNAG_02565 gene results in lysine auxotrophy. The lys4 mutant shows increased sensitivity to oxidative stress, agents that challenge cell wall/membrane integrity, and azole antifungal drugs. The phenotype is due in part to impaired mitochondrial function as a result of LYS4 deletion, which disrupts iron homeostasis in the organelle. The lys4 mutant is attenuated virulence in a mouse inhalation model of cryptococcosis. Loss of the enzyme results in organelle dysfunction due to a potential impact on Fe-S levels
malfunction
Cryptococcus neoformans var. grubii serotype A H99 / ATCC 208821 / CBS 10515 / FGSC 9487
-
deletion of the CNAG_02565 gene results in lysine auxotrophy. The lys4 mutant shows increased sensitivity to oxidative stress, agents that challenge cell wall/membrane integrity, and azole antifungal drugs. The phenotype is due in part to impaired mitochondrial function as a result of LYS4 deletion, which disrupts iron homeostasis in the organelle. The lys4 mutant is attenuated virulence in a mouse inhalation model of cryptococcosis. Loss of the enzyme results in organelle dysfunction due to a potential impact on Fe-S levels
-
physiological function
Cryptococcus neoformans var. grubii serotype A
the enzyme expression is regulated by iron levels and by the iron-related transcription factors Hap3 and HapX. The enzyme is essential for lysine biosynthesis and is required for full virulence. The iron metabolism and homeostasis have a large influence on the virulence of Cryptococcus neoformans
physiological function
Cryptococcus neoformans var. grubii serotype A H99 / ATCC 208821 / CBS 10515 / FGSC 9487
-
the enzyme expression is regulated by iron levels and by the iron-related transcription factors Hap3 and HapX. The enzyme is essential for lysine biosynthesis and is required for full virulence. The iron metabolism and homeostasis have a large influence on the virulence of Cryptococcus neoformans
-
Show AA Sequence and Transmembrane Helices (307 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
heterotetramer, MJ1003 and MJ1271 proteins form an active homoaconitase enzyme
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sitting-drop vapour-diffusion method and hanging-drop vapour diffusion at 20°C, structures of the large subunit of homoaconise is reported at 2.5 A resolution
small-subunit HACN protein (MJ1271), micro batch method, using 50% (w/v) polyethylene glycol 200 and 0.1 M Tris-HCl, pH 4.6, at 20°C
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
R26K
-
the variant forms an relatively efficient isopropylmalate isomerase enzyme
R26V
-
the variant forms an relatively efficient isopropylmalate isomerase enzyme
R26V/T27Y
-
the variant resembles the MJ1277 isopropylmalate isomerase small subunit in its flexible loop sequence but demonstrates the broad substrate specificity of the R26V variant
T27A t
-
the variant has uniformly lower specificity constants for both isopropylmalate isomerase and methanogen homoaconitase substrates
additional information
additional information
Cryptococcus neoformans var. grubii serotype A
generation of a CNAG_02565 deletion mutant, the deletion impairs mitochondrial functions, phenotype, overview
additional information
Cryptococcus neoformans var. grubii serotype A H99 / ATCC 208821 / CBS 10515 / FGSC 9487
-
generation of a CNAG_02565 deletion mutant, the deletion impairs mitochondrial functions, phenotype, overview
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant MJ1003 and MJ1271 proteins from Escherichia coli strain BL21(DE3) by heat treatment of the cell lysate, followed by anion exchange chromatography, dialysis, and ultrafiltration
Toyopearl SuperQ-650 M column chromatography, Resource S column chromatography, and Superdex 200 gel filtration
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, coexpression of MJ1003 and MJ1271 proteins in Escherichia coli strain BL21(DE3)
recombinant expression of GFP-tagged enzyme targeted to mitochondria
Cryptococcus neoformans var. grubii serotype A
small-subunit HACN protein MJ1271 is expressed in Escherichia coli BL21 CodonPlus (DE3)-RIL cells
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the gene CNAG_02565 is significantly downregulated in the cfo1 mutant
the gene CNAG_02565 is significantly downregulated in the cfo1 mutant
Cryptococcus neoformans var. grubii serotype A
the gene CNAG_02565 is significantly downregulated in the cfo1 mutant
Cryptococcus neoformans var. grubii serotype A H99 / ATCC 208821 / CBS 10515 / FGSC 9487
-
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug development
drug development
Cryptococcus neoformans var. grubii serotype A
the enzyme is a possible antifungal drug target
drug development
Cryptococcus neoformans var. grubii serotype A H99 / ATCC 208821 / CBS 10515 / FGSC 9487
-
the enzyme is a possible antifungal drug target
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Drevland, R.M.; Jia, Y.; Palmer, D.R.; Graham, D.E.
Methanogen homoaconitase catalyzes both hydrolyase reactions in coenzyme B biosynthesis
J. Biol. Chem.
283
28888-28896
2008
Methanocaldococcus jannaschii, Methanocaldococcus jannaschii (Q58991)
brenda
Jeyakanthan, J.; Drevland, R.M.; Gayathri, D.R.; Velmurugan, D.; Shinkai, A.; Kuramitsu, S.; Yokoyama, S.; Graham, D.E.
Substrate specificity determinants of the methanogen homoaconitase enzyme: structure and function of the small subunit
Biochemistry
49
2687-2696
2010
Methanocaldococcus jannaschii
brenda
Lee, E.H.; Lee, K.; Hwang, K.Y.
Structural characterization and comparison of the large subunits of IPM isomerase and homoaconitase from Methanococcus jannaschii
Acta Crystallogr. Sect. D
70
922-931
2014
Methanocaldococcus jannaschii (Q58409), Methanocaldococcus jannaschii, Methanocaldococcus jannaschii DSM 2661 (Q58409)
brenda
Do, E.; Park, M.; Hu, G.; Caza, M.; Kronstad, J.W.; Jung, W.H.
The lysine biosynthetic enzyme Lys4 influences iron metabolism, mitochondrial function and virulence in Cryptococcus neoformans
Biochem. Biophys. Res. Commun.
477
706-711
2016
Cryptococcus neoformans var. grubii serotype A (J9VIU5), Cryptococcus neoformans var. grubii serotype A H99 / ATCC 208821 / CBS 10515 / FGSC 9487 (J9VIU5)
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