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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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4.3.1.17 L-serine ammonia-lyaseIUBMB 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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Word Map
- 4.3.1.17
- aminotransferase
- pyridoxal
-
deamination
- glucagon
-
gluconeogenesis
-
gluconeogenic
- hydroxymethyltransferase
- l-isoleucine
- d-serine
-
plp-dependent
-
peptostreptococcus
- deaminases
- 2-oxobutyrate
- asaccharolyticus
- analysis
- medicine
The taxonomic range for the selected organisms is: Mus musculus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
serine dehydratase, l-serine dehydratase, l-threonine deaminase, l-threonine dehydratase, l-serine deaminase, serine deaminase, serdh, lplsd, l-sd2, msmeg_3532, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Dehydratase, L-serine
-
-
-
-
L-Hydroxy amino acid dehydratase
-
-
-
-
L-SD
-
-
-
-
L-SD1
-
-
-
-
L-SD2
-
-
-
-
L-Serine deaminase
-
-
-
-
SD
-
-
-
-
SDH
-
-
-
-
Serine deaminase
-
-
-
-
Serine dehydratase
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
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
9014-27-1
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
racemization and elimination activities reside at the same active site of enzyme. Racemization activity is specific to serine, elimination activity has a broader specificity for L-amino acids with a suitable leaving group at the beta-carbon
-
-
?
additional information
?
-
-
ration of elimination reaction/racemization reaction for substrate L-serine is 3.7
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ATP
-
inhibitory to L-serine O-sulfate dehydration reaction, activating for racemization reraction
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.49
L-serine O-sulfate
pH 8.0, 37°C, presence of 1 mM ATP, elimination reaction
12
D-serine
-
mutant Q155D, alpha,beta-elimination, presence of ATP, pH 7.4, 37°C
55
D-threonine
-
wild-type, alpha,beta-elimination, presence of ATP, pH 7.4, 37°C
60
D-threonine
-
mutant Q155D, alpha,beta-elimination, presence of ATP, pH 7.4, 37°C
11
L-serine
-
mutant Q155D, alpha,beta-elimination, presence of ATP, pH 7.4, 37°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.6
beta-chloro-L-alanine
pH 8.0, 37°C, presence of 1 mM ATP, elimination reaction
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
0.012
D-serine
-
mutant Q155D, alpha,beta-elimination, presence of ATP, pH 7.4, 37°C
0.042
D-serine
-
wild-type, alpha,beta-elimination, presence of ATP, pH 7.4, 37°C
0.028
D-threonine
-
mutant Q155D, alpha,beta-elimination, presence of ATP, pH 7.4, 37°C
0.3
D-threonine
-
wild-type, alpha,beta-elimination, presence of ATP, pH 7.4, 37°C
0.166
L-serine
-
wild-type, alpha,beta-elimination, presence of ATP, pH 7.4, 37°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
bifunctional enzyme, racemization of serine and elimination of L-serine and L-serine-O-sulfate to form pyruvate
Swissprot
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). SRR_MOUSE
339
0
36359
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
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
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)
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)
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
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