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Information on EC 4.1.2.13 - fructose-bisphosphate aldolase and Organism(s) Mycobacterium tuberculosis and UniProt Accession P9WQA3
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4.1.2.13 fructose-bisphosphate aldolaseIUBMB Comments
Also acts on (3S,4R)-ketose 1-phosphates. The yeast and bacterial enzymes are zinc proteins. The enzymes increase electron-attraction by the carbonyl group, some (Class I) forming a protonated imine with it, others (Class II), mainly of microbial origin, polarizing it with a metal ion, e.g. zinc.
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Word Map
- 4.1.2.13
- creatine
-
phosphofructokinase
- enolase
- hexokinase
- isozyme
- isoenzymes
- dihydroxyacetone
- glucose-6-phosphate
- erythrocyte
- phosphoglycerate
- aminotransferase
- albumin
- transaminase
- malate
- intolerance
- gapdh
- hereditary
- muscular
-
phosphokinase
- glycogen
- pentose
- myopathy
- plasmodium
-
gluconeogenesis
-
schiff
- falciparum
- transketolase
- phosphoglucomutase
-
purkinje
- dermatomyositis
- mutase
-
phosphoglucose
-
entner-doudoroff
- dhap
- myositis
- 6-phosphogluconate
-
gluconeogenic
-
calvin
- myoglobin
- myalgia
- fructose-1,6-bisphosphatase
- tpi
- rhabdomyolysis
- polymyositis
- fbpase
- fructokinase
- medicine
-
electromyography
- glycosomal
-
parasagittal
-
glutamic-oxalacetic
- molecular biology
- drug development
- diagnostics
- food industry
- agriculture
- synthesis
The taxonomic range for the selected organisms is: Mycobacterium tuberculosis
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
aldolase, aldolase a, aldolase b, aldolase c, aldoa, fructose-1,6-bisphosphate aldolase, fructose-bisphosphate aldolase, aldob, fructose bisphosphate aldolase, fructose 1,6-bisphosphate aldolase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
1,6-Diphosphofructose aldolase
-
-
-
-
37 kDa major allergen
-
-
-
-
41 kDa antigen
-
-
-
-
aldolase
-
-
-
-
aldolase, fructose diphosphate
-
-
-
-
ALDP
-
-
-
-
Brain-type aldolase
-
-
-
-
CE1
-
-
-
-
CE2
-
-
-
-
Diphosphofructose aldolase
-
-
-
-
FBP aldolase
Fru-P2A
-
-
-
-
Fructoaldolase
-
-
-
-
Fructose 1,6-bisphosphate aldolase
-
-
-
-
Fructose 1,6-diphosphate aldolase
-
-
-
-
Fructose 1-monophosphate aldolase
-
-
-
-
Fructose 1-phosphate aldolase
-
-
-
-
Fructose bisphosphate aldolase
-
-
-
-
Fructose diphosphate aldolase
-
-
-
-
Fructose-1,6-bisphosphate triosephosphate-lyase
-
-
-
-
IgE-binding allergen
-
-
-
-
ketose 1-phosphate aldolase
-
-
-
-
Liver-type aldolase
-
-
-
-
Muscle-type aldolase
-
-
-
-
Phosphofructoaldolase
-
-
-
-
SMALDO
-
-
-
-
zymohexase
-
-
-
-
FBP aldolase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
condensation
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
-
-, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
D-fructose-1,6-bisphosphate D-glyceraldehyde-3-phosphate-lyase (glycerone-phosphate-forming)
Also acts on (3S,4R)-ketose 1-phosphates. The yeast and bacterial enzymes are zinc proteins. The enzymes increase electron-attraction by the carbonyl group, some (Class I) forming a protonated imine with it, others (Class II), mainly of microbial origin, polarizing it with a metal ion, e.g. zinc.
CAS REGISTRY NUMBER
COMMENTARY
9024-52-6
-
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
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
dihydroxyacetone phosphate + D-glyceraldehyde 3-phosphate
D-fructose 1,6-bisphosphate
-
-
-
r
D-Fructose 1-phosphate
Glycerone phosphate + D-glyceraldehyde
-
no activity
-
-
?
D-fructose-1,6-bisphosphate
dihydroxyacetone phosphate + glyceraldehyde-3-phosphate
-
-
-
-
?
D-fructose-1,6-bisphosphate
dihydroxyacetone phosphate + glyceraldehyde-3-phosphate
-
-
-
?
D-fructose-1,6-bisphosphate
dihydroxyacetone phosphate + glyceraldehyde-3-phosphate
-
-
-
r
D-fructose 1,6-bisphosphate
dihydroxyacetone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
dihydroxyacetone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
r
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
additional information
?
-
similar to other Class II FBA, neither fructose 1-phosphate nor fructose 6-phosphate (up to 50 mM each) act as substrates for both rMtFBA
-
-
?
additional information
?
-
product glycerone phosphate is leaving first followed by dihydroxyacetone phosphate in a uni-bi kinetic scheme
-
-
?
additional information
?
-
-
product glycerone phosphate is leaving first followed by dihydroxyacetone phosphate in a uni-bi kinetic scheme
-
-
?
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
D-fructose-1,6-bisphosphate
dihydroxyacetone phosphate + glyceraldehyde-3-phosphate
-
-
-
r
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
Cu2+
addition of Cu2+, Fe2+, Ni2+, Mg2+, and Mn2+ leads to only a small level of recovery of activity
Fe2+
addition of Cu2+, Fe2+, Ni2+, Mg2+, and Mn2+ leads to only a small level of recovery of activity
Mg2+
addition of Cu2+, Fe2+, Ni2+, Mg2+, and Mn2+ leads to only a small level of recovery of activity
Mn2+
addition of Cu2+, Fe2+, Ni2+, Mg2+, and Mn2+ leads to only a small level of recovery of activity
Ni2+
addition of Cu2+, Fe2+, Ni2+, Mg2+, and Mn2+ leads to only a small level of recovery of activity
Zn2+
Zn2+
Co2+
addition of only Co2+ and Zn2+ can recover the activity to higher than half of the original
Zn2+
the native recombinant enzyme is zinc-dependent, contains 0.5 Zn2+ per monomer
Zn2+
addition of only Co2+ and Zn2+ can recover the activity to higher than half of the original
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-propanol
at 12.5% (v/v) remaining activity, 69.99%, and 25% (v/v) remaining activity, 3.72%
Benzene
at 12.5% (v/v) remaining activity, 88.94%, and 25% (v/v) remaining activity, 88.94%
dihydroxyacetone phosphate
competitive with fructose 1,6-bisphosphate
dimethylsulfoxid
at 12.5% (v/v) remaining activity, 131.26%, and 25% (v/v) remaining activity, 133.2%
ethanol
at 12.5% (v/v) remaining activity, 79.19%, and 25% (v/v) remaining activity, 33.41%
ethyl acetate
at 12.5% (v/v) remaining activity, 71.96%, and 25% (v/v) remaining activity, 41.62%
hexane
at 12.5% (v/v) remaining activity, 98.25%, and 25% (v/v) remaining activity, 92.22%
N,N-dimethylmethanamide
at 12.5% (v/v) remaining activity, 118.40%, and 25% (v/v) remaining activity, 73.93%
N-(3-hydroxypropyl)-glycolohydrazide-bisphosphate
fructose-1,6-bisphosphate analogue
N-(3-hydroxypropyl)-glycolohydroxamic acid bisphosphate
fructose-1,6-bisphosphate analogue, weakly active
N-(3-hydroxypropyl)-phosphoglycolohydroxamic acid
fructose-1,6-bisphosphate analogue
N-(4-hydroxybutyl)-glycolohydroxamic acid bisphosphate
inhibitor attachment has no effect on the plasminogen binding activity of the enzyme but competes with the natural substrate, fructose 1,6-bisphosphate, and substantiates a reaction mechanism associated with metallodependent aldolases involving recruitment of the catalytic zinc ion by the substrate upon active site binding
phosphoglycoloamidoxime
dihydroxyacetone phosphate analogue
phosphoglycolohydrazide
dihydroxyacetone phosphate analogue
Phosphoglycolohydroxamate
use as a mimic of the hydroxyenolate intermediate- and dihydroxyacetone phosphate-bound form of the enzyme
Toluene
at 12.5% (v/v) remaining activity, 89.70%, and 25% (v/v) remaining activity, 91.02%
2-carboxy-6-(phosphonomethyl)pyridinium chloride
-
metal-chelating inhibitor
2-[hydroxy(3-hydroxypropyl)amino]-2-oxoethyl dihydrogen phosphate
-
-
2-[hydroxy(4-hydroxybutyl)amino]-2-oxoethyl dihydrogen phosphate
-
-
3-[hydroxy[(phosphonooxy)acetyl]amino]propyl dihydrogen phosphate
-
-
additional information
all methyl 4-oxo-2-butenoates, 3-hydroxy-2-pyrrolones, 1,4-bezoxazines and compounds containing 4-quinolone fragment does not inhibit rMtFBA
-
EDTA
-
the activity of the EDTA-inactivated enzyme increases more than 6fold upon the addition of 0.002 mM Zn2+ and increases by a factor 2 with the addition of 0.002 mM Co2+. The addition of Cu2+, Ni2+, Cd2+, Mn2+, or Mg2+ does not reactivate the enzyme significantly
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-mercaptoethanol
sulfhydryl compound such as 2-mercaptoethanol, activates the C-His-rMtFBA activity slightly, 15%
dithiothreitol
sulfhydryl compound such as dithiothreitol, activates the C-His-rMtFBA activity slightly, 25%
additional information
1 mM PMSF has no effect on the enzyme activity
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.01503
D-fructose-1,6-bisphosphate
purified C-His-rMtFBA, indicates that the extra five histidine residues in C-His-rMtFBA has negligible effects on the kinetic properties of the enzyme
0.018
D-fructose-1,6-bisphosphate
mutant E169A, pH 7.8, 22°C
0.021
D-fructose-1,6-bisphosphate
mutant G167A, pH 7.8, 22°C
0.021
D-fructose-1,6-bisphosphate
mutant G167A/G166A, pH 7.8, 22°C
0.03
D-fructose-1,6-bisphosphate
mutant E168A, pH 7.8, 22°C
0.18
D-fructose-1,6-bisphosphate
mutant D276A, pH 7.8, 22°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.01
D-fructose-1,6-bisphosphate
mutant E169A, pH 7.8, 22°C
0.11
D-fructose-1,6-bisphosphate
mutant G167A/G166A, pH 7.8, 22°C
0.17
D-fructose-1,6-bisphosphate
mutant G167A, pH 7.8, 22°C
0.45
D-fructose-1,6-bisphosphate
mutant D276A, pH 7.8, 22°C
2.67
D-fructose-1,6-bisphosphate
mutant E168A, pH 7.8, 22°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.28
D-fructose-1,6-bisphosphate
mutant E169A, pH 7.8, 22°C
5.33
D-fructose-1,6-bisphosphate
mutant G167A/G166A, pH 7.8, 22°C
88.33
D-fructose-1,6-bisphosphate
mutant E168A, pH 7.8, 22°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00031
2-(3-hydroxy-2-oxo-1,2-dihydropyridin-4-yl)ethyl phosphate
-
in glycyl-glycine buffer (0.1 M pH 7.4), temperature not specified in the publication
0.00017
2-[hydroxy(3-hydroxypropyl)amino]-2-oxoethyl dihydrogen phosphate
-
in glycyl-glycine buffer (0.1 M pH 7.4), temperature not specified in the publication
0.000185
2-[hydroxy(4-hydroxybutyl)amino]-2-oxoethyl dihydrogen phosphate
-
in glycyl-glycine buffer (0.1 M pH 7.4), temperature not specified in the publication
0.000013
3-[hydroxy[(phosphonooxy)acetyl]amino]propyl dihydrogen phosphate
-
in glycyl-glycine buffer (0.1 M pH 7.4), temperature not specified in the publication
0.00012
4-[hydroxy[(phosphonooxy)acetyl]amino]butyl hexanoate
-
in glycyl-glycine buffer (0.1 M pH 7.4), temperature not specified in the publication
0.1824
5-chloro-8-hydroxyquinoline
native-rMtFBA, Ki = 182.4 microM and KI = 219.5 microM
0.1934
5-chloro-8-hydroxyquinoline
C-His-rMtFBA, Ki = 193.4 microM and KI = 220.9 microM. This indicates a possible use of C-His-rMtFBA for screening of MtFBA inhibitors
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.057
2-carboxy-6-(phosphonomethyl)pyridinium chloride
Mycobacterium tuberculosis
-
pH 7.3, 28°C
0.33
5-chloro-8-hydroxyquinoline
Mycobacterium tuberculosis
NADH-linked enzymatic assay
0.533
5-chloro-8-hydroxyquinoline
Mycobacterium tuberculosis
determined by the colorimetric assay
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.3 - 8.5
pH 7.3: about 70% of maximal activity, pH 8.5: about 55% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.6
native-rMtFBA, agreeing with the calculation from their sequence, 5.42
5.9
C-His-rMtFBA, agreeing with the calculation from their sequence, 5.82
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
gene product is required for the growth of Mycobacterium tuberculosis on gluconeogenetic substrates and in glucose-containing medium
metabolism
-
the enzyme is involved in the Embden-Meyerhof-Parnas glycolytic pathway and in gluconeogenesis
physiological function
-
conserved glycolytic enzyme with virulence functions in bacteria. It is involved in the Embden-Meyerhof-Parnas (EMP) glycolytic pathway and in gluconeogenesis. Additional it functions beyond its housekeeping role in central metabolism. The enzyme from Mycobacterium tuberculosis binds human plasminogen
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complex with inhibitor phosphoglycolohydroxamate as a mimic of the hydroxyenolate intermediate- and dihydroxyacetone phosphate-bound form of the enzyme, to 1.58 A resolution. Residue E169 facilitates a water-mediated deprotonation-protonation step of the reaction mechanism
native form and in complex with a hydroxamate substrate analog, to 2.35- and 1.9 A resolution, respectively. Inhibitor attachment has no effect on the plasminogen binding activity of the enzyme, it competes with the natural substrate, fructose 1,6-bisphosphate, and substantiates a reaction mechanism associated with metallodependent aldolases involving recruitment of the catalytic zinc ion by the substrate upon active site binding
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 10
C-His-rMtFBA and native-rMtFBA are stable in a wider pH range of 7.0-10.0
692126
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60
-
the aldolase loses almost all its activity after a 10 min incubation at 60°C
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
stored in the 50 mM Tris-HCl buffer, pH 7.4 containing 1 mM 2-mercaptoethanol and 100 microM ZnCl2, stable at 4°C for over 10 months without significant loss of activity.
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acetone
-
more than 50% of the enzyme activity is retained in the presence of 25% (v/v) acetone
acetonitrile
-
more than 50% of the enzyme activity is retained in the presence of 10% (v/v) acetonitrile
dimethylformamide
-
more than 50% of the enzyme activity is retained in the presence of 20% (v/v) dimethylformamide
DMSO
-
more than 50% of the enzyme activity is retained in the presence of 50% (v/v) DMSO
tert-Butanol
-
more than 50% of the enzyme activity is retained in the presence of 20% (v/v) tert-butanol
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
immobilized metal affinity chromatography, Ni2+-IDA affinity chromatography
ammonium sulfate precipitation, DEAE Sepharose column chromatography, and Sepharose Q column chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed C-terminal histidine-tagged Class II FBA is produced in Escherichia coli BL21
subcloned in the Escherichia coli vector pT7-7. Attempts to express the enzyme with an N-terminal fusion tag yields inactive, mostly insoluble protein
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
protein is produced under various axenic growth conditions including oxygen depletion and hence by non-replicating bacilli, and also in vivo in the lungs of infected guinea pigs and mice. Enzyme binds human plasmin(ogen) and protects bound plasmin from regulation by alpha2-antiplasmin
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Jayanthi Bai, N.; Ramachandra Pai, M.; Suryanarayana Murthy, P.; Venkitasubramanian, T.A.
Fructose-bisphosphate aldolases from Mycobacteria
Methods Enzymol.
90
241-250
1982
Mycobacterium tuberculosis, Mycolicibacterium smegmatis
Ramsaywak, P.C.; Labbe, G.; Siemann, S.; Dmitrienko, G.I.; Guillemette, J.G.
Molecular cloning, expression, purification, and characterization of fructose 1,6-bisphosphate aldolase from Mycobacterium tuberculosis--a novel class II A tetramer
Protein Expr. Purif.
37
220-228
2004
Mycobacterium tuberculosis (P9WQA3), Mycobacterium tuberculosis H37Rv (P9WQA3), Mycobacterium tuberculosis H37Rv
Fonvielle, M.; Coincon, M.; Daher, R.; Desbenoit, N.; Kosieradzka, K.; Barilone, N.; Gicquel, B.; Sygusch, J.; Jackson, M.; Therisod, M.
Synthesis and biochemical evaluation of selective inhibitors of class II fructose bisphosphate aldolases: towards new synthetic antibiotics
Chemistry
14
8521-8529
2008
Oryctolagus cuniculus (P00883), Saccharomyces cerevisiae (P14540), Helicobacter pylori (P56109), Mycobacterium tuberculosis (P9WQA3), Mycobacterium tuberculosis H37Rv (P9WQA3)
Rukseree, K.; Thammarongtham, C.; Palittapongarnpim, P.
One-step purification and characterization of a fully active histidine-tagged Class II fructose-1,6-bisphosphate aldolase from Mycobacterium tuberculosis
Enzyme Microb. Technol.
43
500-506
2008
Mycobacterium tuberculosis (P9WQA3), Mycobacterium tuberculosis H37Rv (P9WQA3)
-
Pegan, S.D.; Rukseree, K.; Franzblau, S.G.; Mesecar, A.D.
Structural basis for catalysis of a tetrameric class IIa fructose 1,6-bisphosphate aldolase from Mycobacterium tuberculosis
J. Mol. Biol.
386
1038-1053
2009
Mycobacterium tuberculosis (P9WQA3), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WQA3)
Daher, R.; Coincon, M.; Fonvielle, M.; Gest, P.M.; Guerin, M.E.; Jackson, M.; Sygusch, J.; Therisod, M.
Rational design, synthesis, and evaluation of new selective inhibitors of microbial class II (zinc dependent) fructose bis-phosphate aldolases
J. Med. Chem.
53
7836-7842
2010
Candida albicans, Oryctolagus cuniculus, Helicobacter pylori, Mycobacterium tuberculosis, Yersinia pestis
Labbe, G.; de Groot, S.; Rasmusson, T.; Milojevic, G.; Dmitrienko, G.I.; Guillemette, J.G.
Evaluation of four microbial Class II fructose 1,6-bisphosphate aldolase enzymes for use as biocatalysts
Protein Expr. Purif.
80
224-233
2011
Bacillus cereus, Pyricularia grisea, Mycobacterium tuberculosis, Pseudomonas aeruginosa, Bacillus cereus ATCC 10987
Pegan, S.D.; Rukseree, K.; Capodagli, G.C.; Baker, E.A.; Krasnykh, O.; Franzblau, S.G.; Mesecar, A.D.
Active site loop dynamics of a class IIa fructose 1,6-bisphosphate aldolase from Mycobacterium tuberculosis
Biochemistry
52
912-925
2013
Mycobacterium tuberculosis (P9WQA3), Mycobacterium tuberculosis
de la Paz Santangelo, M.; Gest, P.M.; Guerin, M.E.; Coincon, M.; Pham, H.; Ryan, G.; Puckett, S.E.; Spencer, J.S.; Gonzalez-Juarrero, M.; Daher, R.; Lenaerts, A.J.; Schnappinger, D.; Therisod, M.; Ehrt, S.; Sygusch, J.; Jackson, M.
Glycolytic and non-glycolytic functions of Mycobacterium tuberculosis fructose-1,6-bisphosphate aldolase, an essential enzyme produced by replicating and non-replicating bacilli
J. Biol. Chem.
286
40219-40231
2011
Mycobacterium tuberculosis (P9WQA3), Mycobacterium tuberculosis
Labbe, G.; Krismanich, A.P.; de Groot, S.; Rasmusson, T.; Shang, M.; Brown, M.D.; Dmitrienko, G.I.; Guillemette, J.G.
Development of metal-chelating inhibitors for the class II fructose 1,6-bisphosphate (FBP) aldolase
J. Inorg. Biochem.
112
49-58
2012
Bacillus cereus, Pyricularia grisea, Mycobacterium tuberculosis, Pseudomonas aeruginosa
Shams, F.; Oldfield, N.J.; Wooldridge, K.G.; Turner, D.P.
Fructose-1,6-bisphosphate aldolase (FBA)-a conserved glycolytic enzyme with virulence functions in bacteria 'ill met by moonlight
Biochem. Soc. Trans.
42
1792-1795
2014
Streptococcus pneumoniae, Mycobacterium tuberculosis, Neisseria meningitidis, Streptococcus suis, Streptococcus suis SS9, Streptococcus pneumoniae WU2
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