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

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 4.1.3.3 - N-acetylneuraminate lyase and Organism(s) Staphylococcus carnosus and UniProt Accession B9DIJ2

for references in articles please use BRENDA:EC4.1.3.3
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.3 Oxo-acid-lyases
                4.1.3.3 N-acetylneuraminate lyase
IUBMB Comments
This enzyme is involved in the degradation of N-acetylneuraminate. It is specific for the open form of the sugar. It also acts on N-glycoloylneuraminate and on O-acetylated sialic acids, other than 4-O-acetylated derivatives.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Staphylococcus carnosus
UNIPROT: B9DIJ2
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
hide
The taxonomic range for the selected organisms is: Staphylococcus carnosus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
n-acetylneuraminate lyase, sialic acid aldolase, n-acetylneuraminic acid aldolase, n-acetylneuraminic acid lyase, neu5ac aldolase, n-acetyl-d-neuraminic acid aldolase, neuac lyase, n-acetylneuraminate pyruvate lyase, n-acetylneuraminate pyruvate-lyase, neuraminic acid aldolase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acetylneuraminate pyruvate-lyase
-
-
-
-
Lyase, acetylneuraminate
-
-
-
-
N-Acetylneuraminate aldolase
-
-
-
-
N-Acetylneuraminate lyase
-
-
-
-
N-acetylneuraminate pyruvate lyase
-
-
-
-
N-Acetylneuraminate pyruvate-lyase
-
-
-
-
N-Acetylneuraminic acid aldolase
-
-
-
-
N-Acetylneuraminic acid lyase
-
-
-
-
N-Acetylneuraminic aldolase
-
-
-
-
N-Acetylneuraminic lyase
-
-
-
-
NALase
-
-
-
-
NANA lyase
-
-
-
-
NeuAc aldolase
-
-
-
-
Neuraminate aldolase
-
-
-
-
Neuraminic acid aldolase
-
-
-
-
Neuraminic aldolase
-
-
-
-
NPL
-
-
-
-
Sialate lyase
-
-
-
-
Sialic acid aldolase
-
-
-
-
Sialic aldolase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
condensation
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
aceneuramate pyruvate-lyase (N-acetyl-D-mannosamine-forming)
This enzyme is involved in the degradation of N-acetylneuraminate. It is specific for the open form of the sugar. It also acts on N-glycoloylneuraminate and on O-acetylated sialic acids, other than 4-O-acetylated derivatives.
CAS REGISTRY NUMBER
COMMENTARY hide
9027-60-5
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
N-acetyl-D-mannosamine + pyruvate
N-acetylneuraminate
show the reaction diagram
reversible aldol condensation of pyruvate and N-acetyl-D-mannosamine
-
-
r
N-acetylneuraminate
N-acetyl-D-mannosamine + pyruvate
show the reaction diagram
-
-
-
r
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
N-acetyl-D-mannosamine + pyruvate
N-acetylneuraminate
show the reaction diagram
reversible aldol condensation of pyruvate and N-acetyl-D-mannosamine
-
-
r
N-acetylneuraminate
N-acetyl-D-mannosamine + pyruvate
show the reaction diagram
-
-
-
r
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
149
N-acetyl-D-mannosamine
recombinant His-taggged enzyme, pH 7.0, 37°C
2
N-acetylneuraminate
recombinant His-taggged enzyme, pH 7.0, 37°C
1 - 4
pyruvate
recombinant His-taggged enzyme, pH 7.0, 37°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4.5
N-acetyl-D-mannosamine
recombinant His-taggged enzyme, pH 7.0, 37°C
4
N-acetylneuraminate
recombinant His-taggged enzyme, pH 7.0, 37°C
2.9
pyruvate
recombinant His-taggged enzyme, pH 7.0, 37°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.03
N-acetyl-D-mannosamine
recombinant His-taggged enzyme, pH 7.0, 37°C
2
N-acetylneuraminate
recombinant His-taggged enzyme, pH 7.0, 37°C
0.21
pyruvate
recombinant His-taggged enzyme, pH 7.0, 37°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
12.7
purified recombinant His-taggged enzyme, pH 7.0, 37°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
synthesis reaction
60
hydrolysis reaction
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 80
synthesis and hydrolysis reactions, profiles, overview
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 50
purified recombinant His-tagged enzyme, pH 7.0, completely stable over 140-160 min
60
purified recombinant His-tagged enzyme, pH 7.0, 120 min, 60% activity remaining
70
purified recombinant His-tagged enzyme, pH 7.0, inactivation within 60 min
80
purified recombinant His-tagged enzyme, pH 7.0, inactivation within 10 min
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme 7.5fold from Escherichia coli strain Rosetta (DE3) pLys by ultrafiltration, nickel affinity chromatography, and gel filtration, to homogeneity
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene ScNAL, sequence comparison, expression of His-tagged enzyme in Escherichia coli strain Rosetta (DE3) pLys
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
the enzyme can be a useful and cheap biocatalyst to produce N-acetylneuraminic acid (Neu5Ac)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Garcia Garcia, M.I.; Sola Carvajal, A.; Garcia Carmona, F.; Sanchez Ferrer, A.
Characterization of a novel N-acetylneuraminate lyase from Staphylococcus carnosus TM300 and its application to N-acetylneuraminic acid production
J. Agric. Food Chem.
60
7450-7456
2012
Staphylococcus carnosus (B9DIJ2), Staphylococcus carnosus TM300 (B9DIJ2), Staphylococcus carnosus TM300
Manually annotated by BRENDA team