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Information on EC 4.3.1.17 - L-serine ammonia-lyase and Organism(s) Mus musculus and UniProt Accession Q9QZX7

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EC Tree
     4 Lyases
         4.3 Carbon-nitrogen lyases
             4.3.1 Ammonia-lyases
                4.3.1.17 L-serine ammonia-lyase
IUBMB Comments
Most enzymes that catalyse this reaction are pyridoxal-phosphate-dependent, although some enzymes contain an iron-sulfur cluster instead . The reaction catalysed by both types of enzymes involves the initial elimination of water to form an enamine intermediate (hence the enzyme's original classification as EC 4.2.1.13, L-serine dehydratase), followed by tautomerization to an imine form and hydrolysis of the C-N bond. The latter reaction, which can occur spontaneously, is also be catalysed by EC 3.5.99.10, 2-iminobutanoate/2-iminopropanoate deaminase. This reaction is also carried out by EC 4.3.1.19, threonine ammonia-lyase, from a number of sources.
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This record set is specific for:
Mus musculus
UNIPROT: Q9QZX7
Word Map
The taxonomic range for the selected organisms is: Mus musculus
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
hide(Overall reactions are displayed. Show all >>)
Synonyms
bsLSD type 1, cSDH, Dehydratase, L-serine, EC 4.2.1.13, GSU0486, HSDH, L-Hydroxy amino acid dehydratase, L-SD, L-SD1, L-SD2, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Dehydratase, L-serine
-
-
-
-
L-Hydroxy amino acid dehydratase
-
-
-
-
L-SD
-
-
-
-
L-SD1
-
-
-
-
L-SD2
-
-
-
-
L-Serine deaminase
-
-
-
-
SD
-
-
-
-
SDH
-
-
-
-
Serine deaminase
-
-
-
-
Serine dehydratase
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
L-serine ammonia-lyase (pyruvate-forming)
Most enzymes that catalyse this reaction are pyridoxal-phosphate-dependent, although some enzymes contain an iron-sulfur cluster instead [6]. The reaction catalysed by both types of enzymes involves the initial elimination of water to form an enamine intermediate (hence the enzyme's original classification as EC 4.2.1.13, L-serine dehydratase), followed by tautomerization to an imine form and hydrolysis of the C-N bond. The latter reaction, which can occur spontaneously, is also be catalysed by EC 3.5.99.10, 2-iminobutanoate/2-iminopropanoate deaminase. This reaction is also carried out by EC 4.3.1.19, threonine ammonia-lyase, from a number of sources.
CAS REGISTRY NUMBER
COMMENTARY hide
9014-27-1
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
beta-chloro-L-alanine
3-chloropropenoic acid + NH3
show the reaction diagram
-
-
-
?
D-serine
L-serine
show the reaction diagram
D-serine
pyruvate + NH3
show the reaction diagram
L-serine
D-serine
show the reaction diagram
L-serine
pyruvate + NH3
show the reaction diagram
L-serine O-sulfate
O-sulfopyruvate + NH3
show the reaction diagram
elimination reaction
-
-
?
L-serine-O-sulfate
? + NH3
show the reaction diagram
-
elimination reaction
-
-
?
L-threo-3-hydroxyaspartate
oxaloacetate + NH3
show the reaction diagram
-
-
-
?
L-threonine
2-oxobutyrate + NH3
show the reaction diagram
-
-
-
?
L-threonine
3-hydroxy-2-butenoic acid + NH3
show the reaction diagram
-
alpha,beta-elimination reaction
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ATP
-
inhibitory to L-serine O-sulfate dehydration reaction, activating for racemization reraction
Co2+
-
inhibition of both activities
Cu2+
-
inhibition of both activities
EDTA
-
inhibition of both activities
Fe2+
-
slight inhibition of both activities
Ni2+
-
slight inhibition of both activities
Zn2+
-
inhibition of both activities
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.2 - 75
D-serine
55 - 60
D-threonine
3.8 - 75
L-serine
0.49
L-serine O-sulfate
-
pH 8.0, 37°C, presence of 1 mM ATP, elimination reaction
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.6
beta-chloro-L-alanine
-
pH 8.0, 37°C, presence of 1 mM ATP, elimination reaction
0.0033 - 14.5
D-serine
0.028 - 0.3
D-threonine
0.033 - 4
L-serine
0.49
L-serine O-sulfate
-
pH 8.0, 37°C, presence of 1 mM ATP, elimination reaction
31
L-threo-3-hydroxyaspartate
-
pH 8.0, 37°C, presence of 1 mM ATP, elimination reaction
10.5
L-threonine
-
pH 8.0, 37°C, presence of 1 mM ATP, elimination reaction
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8 - 9.5
-
-
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5
-
negligible activity below
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
bifunctional enzyme, racemization of serine and elimination of L-serine and L-serine-O-sulfate to form pyruvate
Swissprot
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
SRR_MOUSE
339
0
36359
Swiss-Prot
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
36121
-
x * 36121, MALDI-MS, x * 36123, calculated
36123
-
x * 36121, MALDI-MS, x * 36123, calculated
37000
-
2 * 37000, SDS-PAGE
55000
-
isoforms A and B, gel filtration
78000
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 36121, MALDI-MS, x * 36123, calculated
dimer
-
2 * 37000, SDS-PAGE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H152S
-
ratio of elimination reaction to racemization is 1.4 compared to 3.7 in wild-type
N154F
-
ratio of elimination reaction to racemization is 0.33 compared to 3.7 in wild-type
P153S
-
ratio of elimination reaction to racemization is 0.24 compared to 3.7 in wild-type
Q155D
-
ratio of elimination reaction to racemization is 0.25 compared to 3.7 in wild-type
PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
both isoforms A and B
-
recombinant enzyme expressed in insect cells
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Strisovsky, K.; Jiraskova, J.; Mikulova, A.; Rulisek, L.; Konvalinka, J.
Dual substrate and reaction specificity in mouse serine racemase: identification of high-affinity dicarboxylate substrate and inhibitors and analysis of the beta-eliminase activity
Biochemistry
44
13091-13100
2005
Mus musculus (Q9QZX7)
Manually annotated by BRENDA team
Strisovsky, K.; Jiraskova, J.; Barinka, C.; Majer, P.; Rojas, C.; Slusher, B.S.; Konvalinka, J.
Mouse brain serine racemase catalyzes specific elimination of L-serine to pyruvate
FEBS Lett.
535
44-48
2003
Mus musculus (Q9QZX7)
Manually annotated by BRENDA team
Foltyn, V.N.; Bendikov, I.; De Miranda, J.; Panizzutti, R.; Dumin, E.; Shleper, M.; Li, P.; Toney, M.D.; Kartvelishvily, E.; Wolosker, H.
Serine racemase modulates intracellular D-serine levels through an alpha,beta-elimination activity
J. Biol. Chem.
280
1754-1763
2005
Mus musculus
Manually annotated by BRENDA team
Neidle, A.; Dunlop, D.S.
Allosteric regulation of mouse brain serine racemase
Neurochem. Res.
27
1719-1724
2002
Mus musculus
Manually annotated by BRENDA team
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