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Information on EC 4.2.1.8 - mannonate dehydratase and Organism(s) Streptococcus suis and UniProt Accession A4VVI4

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EC Tree
     4 Lyases
         4.2 Carbon-oxygen lyases
             4.2.1 Hydro-lyases
                4.2.1.8 mannonate dehydratase
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This record set is specific for:
Streptococcus suis
UNIPROT: A4VVI4 not found.
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Word Map
The taxonomic range for the selected organisms is: Streptococcus suis
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
d-mannonate dehydratase, mannonate dehydratase, mannonate hydrolyase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Altronate hydrolase
-
-
-
-
Altronic hydro-lyase
-
-
-
-
D-mannonate hydrolase
-
-
-
-
D-Mannonate hydrolyase
-
-
-
-
Dehydratase, mannonate
-
-
-
-
Mannonate hydrolyase
-
-
-
-
Mannonic hydrolase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
elimination
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
D-mannonate hydro-lyase (2-dehydro-3-deoxy-D-gluconate-forming)
-
CAS REGISTRY NUMBER
COMMENTARY hide
9024-31-1
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
D-Mannonate
2-Dehydro-3-deoxy-D-gluconate + H2O
show the reaction diagram
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mn2+
each ManD monomer roughly has one Mn2+ ion-binding site
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.9 - 3
D-mannonate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.09 - 5.88
D-mannonate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.047 - 1.96
D-mannonate
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
serotype 2
UniProt
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
41000
2 * 41000, SDS-PAGE
80000
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
2 * 41000, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ManD in native form and in complex with its substrate D-mannonate and Mn2+ ion, hanging drop vapor diffusion method, using 0.2 M potassium-sodium tartrate, 0.1 M sodium citrate (pH 6.5), and 1 M ammonium sulfate (native form) or using 0.2 M potassium sodium tartrate tetrahydrate, 0.1 M trisodium citrate dehydrate (pH 6.5), 1 M ammonium sulfate, and 15 mM D-mannonate
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H311A
the activity of H311A is only 2.4% that of the native wild type enzyme
Y325F
catalytically inactive
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4
ManD exhibits no enzymatic activity at 4°C
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA column chromatography, Superdex 200 gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Zhang, Q.; Gao, F.; Peng, H.; Cheng, H.; Liu, Y.; Tang, J.; Thompson, J.; Wei, G.; Zhang, J.; Du, Y.; Yan, J.; Gao, G.F.
Crystal structures of Streptococcus suis mannonate dehydratase (ManD) and its complex with substrate: genetic and biochemical evidence for a catalytic mechanism
J. Bacteriol.
191
5832-5837
2009
Streptococcus suis (A4VVI4), Streptococcus suis
Manually annotated by BRENDA team