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Information on EC 4.2.1.2 - fumarate hydratase and Organism(s) Arabidopsis thaliana

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EC Tree
     4 Lyases
         4.2 Carbon-oxygen lyases
             4.2.1 Hydro-lyases
                4.2.1.2 fumarate hydratase
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This record set is specific for:
Arabidopsis thaliana
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Word Map
The taxonomic range for the selected organisms is: Arabidopsis thaliana
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
Synonyms
fumarase, fumarate hydratase, fumarase c, class ii fumarase, lmfh-2, scfumc, slfumc, lmfh-1, mmcbc, stfumc, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
fumarase
hydratase, fumarate
-
-
-
-
L-malate hydro-lyase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
elimination
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
(S)-malate hydro-lyase (fumarate-forming)
-
CAS REGISTRY NUMBER
COMMENTARY hide
9032-88-6
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(S)-malate
fumarate + H2O
show the reaction diagram
fumarate + H2O
L-malate
show the reaction diagram
-
-
-
r
L-malate
fumarate + H2O
show the reaction diagram
-
-
-
r
additional information
?
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-oxoglutarate
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.45
(S)-malate
-
0.4 - 0.7
fumarate
0.5 - 1.9
L-malate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
8.5 - 57.6
fumarate
8.5 - 37.8
L-malate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.7
fumarate hydratase reaction
8.2
malate dehydratase reaction
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
FUM1_ARATH
492
0
53000
Swiss-Prot
Mitochondrion (Reliability: 1)
FUM2_ARATH
499
0
54084
Swiss-Prot
other Location (Reliability: 2)
A0A178UQ57_ARATH
499
0
54084
TrEMBL
other Location (Reliability: 2)
B9DFH4_ARATH
492
0
53073
TrEMBL
Mitochondrion (Reliability: 1)
B9DFR5_ARATH
510
0
55766
TrEMBL
other Location (Reliability: 2)
A0A178VMD4_ARATH
492
0
53000
TrEMBL
Mitochondrion (Reliability: 1)
A0A654F412_ARATH
492
0
52988
TrEMBL
Mitochondrion (Reliability: 1)
A0A1P8BDR1_ARATH
408
0
44230
TrEMBL
other Location (Reliability: 2)
A0A178UN34_ARATH
452
0
49059
TrEMBL
other Location (Reliability: 2)
A0A654GAT9_ARATH
499
0
54069
TrEMBL
other Location (Reliability: 2)
B3H477_ARATH
317
0
33729
TrEMBL
other Location (Reliability: 5)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
195000
gel filtration
216000
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
FUM1-green fluorescent protein (GFP) expressed driven by the 35S promoter in Arabidopsis thaliana cell cultures
FUM2-red fluorescent protein (RFP) fusions epressed by the 35S promoter, introduced into Arabidopsis thaliana cell cultures
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
level of FUM2 RNA in rosette leaves is higher in the light than in the dark, but total fumarase activity remains constant throughout the diurnal cycle
the expression of the Fum2 gene is unaffected by phytochrome both in darkness and in light
the main regulator of Fum1 gene transcription, is phytochrome A. The active form of phytochrome A suppresses Fum1 expression. The signal transduction mechanism operates via Ca2+ activation of expression of the gene encoding the transcription factor PIF3, which binds to promoters of phytochrome-regulated genes and inhibits Fum1 expression
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Behal, R.H.; Oliver, D.J.
Biochemical and molecular characterization of fumarase from plants: purification and characterization of the enzyme--cloning, sequencing, and expression of the gene
Arch. Biochem. Biophys.
348
65-74
1997
Pisum sativum, Arabidopsis thaliana (P93033), Arabidopsis thaliana
Manually annotated by BRENDA team
Pracharoenwattana, I.; Zhou, W.; Keech, O.; Francisco, P.B.; Udomchalothorn, T.; Tschoep, H.; Stitt, M.; Gibon, Y.; Smith, S.M.
Arabidopsis has a cytosolic fumarase required for the massive allocation of photosynthate into fumaric acid and for rapid plant growth on high nitrogen
Plant J.
62
785-795
2010
Arabidopsis thaliana (P93033), Arabidopsis thaliana (Q9FI53)
Manually annotated by BRENDA team
Zubimendi, J.P.; Martinatto, A.; Valacco, M.P.; Moreno, S.; Andreo, C.S.; Drincovich, M.F.; Tronconi, M.A.
The complex allosteric and redox regulation of the fumarate hydratase and malate dehydratase reactions of Arabidopsis thaliana fumarase 1 and 2 gives clues for understanding the massive accumulation of fumarate
FEBS J.
285
2205-2224
2018
Arabidopsis thaliana (P93033), Arabidopsis thaliana (Q9FI53), Arabidopsis thaliana
Manually annotated by BRENDA team
Dyson, B.C.; Miller, M.A.; Feil, R.; Rattray, N.; Bowsher, C.G.; Goodacre, R.; Lunn, J.E.; Johnson, G.N.
FUM2, a cytosolic fumarase, is essential for acclimation to low temperature in Arabidopsis thaliana
Plant Physiol.
172
118-127
2016
Arabidopsis thaliana (Q9FI53), Arabidopsis thaliana
Manually annotated by BRENDA team
Eprintsev, A.T.; Fedorin, D.N.; Sazonova, O.V.; Igamberdiev, A.U.
Light inhibition of fumarase in Arabidopsis leaves is phytochrome A-dependent and mediated by calcium
Plant Physiol. Biochem.
102
161-166
2016
Arabidopsis thaliana (P93033), Arabidopsis thaliana (Q9FI53)
Manually annotated by BRENDA team