Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 4.2.1.2 - fumarate hydratase and Organism(s) Corynebacterium glutamicum and UniProt Accession Q8NRN8

for references in articles please use BRENDA:EC4.2.1.2
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
     4 Lyases
         4.2 Carbon-oxygen lyases
             4.2.1 Hydro-lyases
                4.2.1.2 fumarate hydratase
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Corynebacterium glutamicum
UNIPROT: Q8NRN8 not found.
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Corynebacterium glutamicum
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, mmcbc, lmfh-1, stfumc, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
fumarase
-
-
-
-
hydratase, fumarate
-
-
-
-
L-malate hydro-lyase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
elimination
-
-
-
-
C-O bond formation
-
-
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
-
-
-
r
fumaric acid + H2O
L-malic acid
show the reaction diagram
-
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
2 mM, slight stimulation
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(R)-malate
mixed-type inhibition
ATP
competitive or mixed-type inhibition
D-Tartrate
competitive
meso-tartrate
competitive
pyromellitate
competitive
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.4 - 13
(S)-malate
0.38 - 4.2
fumarate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
34 - 460
(S)-malate
310 - 730
fumarate
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5
phosphate buffer, substrate: fumarate
7.5
Tris-HCl buffer, substrate: fumarate
8.3
phosphate buffer, substrate: malate
8.5
Tris-HCl buffer, substrate: malate
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
200000
gel filtration
50000
4 * 50000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
4 * 50000, SDS-PAGE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A227V
3.3-fold improvement of half-life at 50°C and a 3.6°C increase in temperature at which the activity of enzyme decreases by 50% in 15 min compared to the wild-type enzyme
A227V/A411V
half-life at 50°C and temperature at which the activity of enzyme decreases by 50% in 15 min increases to more than 768 min and 52.4°C, respectively
A227V/A411V/E175K
half-life at 50°C increases to more than 2700 min and the temperature at which the activity of enzyme decreases by 50% in 15 min is 9.8°C higher than the wild-type enzyme
A411V
half-life at 50°C increases from 1 min for wild-type to 2.2 min, and the temperature at which the activity of enzyme decreases by 50% in 15 min increases from 44.8°C to 47.2°C
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
44.8
wild-type, 15 min, 50% residual activity
47.2
mutant A411V, 15 min, 50% residual activity
49.4
mutant A227V, 15 min, 50% residual activity
50
half-life of wild-type 1 min, of mutant A411V 2.2 min, of mutant A227V 4.3 min, of mutant A227V/A411V more than 768 min, of mutant A227V/A411V/E175K more than 2700 min
52.4
mutant A227V/A411V, 15 min, 50% residual activity
54.6
mutant A227V/A411V/E175K, 15 min, 50% residual activity
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
dithiothreitol partially restores from urea and alkaline inactivation
enzyme stability is achieved by addition of soy bean protein or bovine serum albumin.
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
use of tryptophan synthase in the generation of L-dihalotryptophans and L-alkynyltryptophans
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Daneel, H.J.; Busse, M.; Faurie, R.
Pharmaceutical grade L-malic acid from fumaric acid - development of an integrated biotransformation and product purification process
Med. Fac. Landbouww. Univ. Gent
61/4a
1333-1340
1996
Corynebacterium glutamicum
-
Manually annotated by BRENDA team
Genda, T.; Watabe, S.; Ozaki, H.
Purification and characterization of fumarase from Corynebacterium glutamicum
Biosci. Biotechnol. Biochem.
70
1102-1109
2006
Corynebacterium glutamicum (Q8NRN8), Corynebacterium glutamicum
Manually annotated by BRENDA team
Lin, L.; Wang, Y.; Wu, M.; Zhu, L.; Yang, L.; Lin, J.
Enhancing the thermostability of fumarase C from Corynebacterium glutamicum via molecular modification
Enzyme Microb. Technol.
115
45-51
2018
Corynebacterium glutamicum (Q8NRN8), Corynebacterium glutamicum, Corynebacterium glutamicum DSM 20300 (Q8NRN8)
Manually annotated by BRENDA team