Any feedback?
Information on EC 4.3.1.17 - L-serine ammonia-lyase and Organism(s) Escherichia coli and UniProt Accession P42630
for references in articles please use BRENDA:EC4.3.1.17Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
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.
Specify your search results
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: Escherichia coli
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
-
-
-
-
Serine deaminase
-
-
-
-
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
L-allo-threonine
2-oxobutyrate + NH3
-
at 4.6% of the rate with L-serine
-
-
?
additional information
?
-
-
no substrate: D-serine. Extremely poor substrate: L-cysteine
-
-
?
NATURAL SUBSTRATE
NATURAL 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
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Iron
Iron
-
7.7 mol iron per mol dimer, two (4Fe-4S)2+ clusters per dimer in anaerobically isolated enzyme, exposure to air results in loss of clusters and concomitant loss of enzyme activity
Iron
-
presence of (4Fe-4S)2+ and of (2Fe-2S)2+ clusters involved in catalytic turnover
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
the enzyme is inactive in crude extract and can be activated with iron and dithiothreitol. The activation requires oxygen, and is inhibited by free radical scavengers and by diethylenentriamine pentaacetic acid, which prevents Fe cycling
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
Escherichia coli K-12 provided with glucose and a mixture of amino acids depletes L-serine more quickly than any other amino acid even in the presence of ammonium sulfate. A mutant lacking 4Fe4S L-serine deaminases SdaA, SdaB, and TdcG is unable to do this. The high level of L-serine that accumulates when the mutant is exposed to amino acid mixtures starves the cells for C1 units and interferes with cell wall synthesis. Growth in minimal medium containing glucose, ammonium sulfate, and Casamino Acids results in deformed cells and frequently lysing, which can be reversed by adding S-adenosylmethionine
physiological function
Escherichia coli K-12 provided with glucose and a mixture of amino acids depletes L-serine more quickly than any other amino acid even in the presence of ammonium sulfate. A mutant lacking 4Fe4S L-serine deaminases SdaA, SdaB, and TdcG is unable to do this. The high level of L-serine that accumulates when the mutant is exposed to amino acid mixtures starves the cells for C1 units and interferes with cell wall synthesis. Growth in minimal medium containing glucose, ammonium sulfate, and Casamino Acids results in deformed cells and frequently lysing, which can be reversed by adding S-adenosylmethionine
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
46000
-
2 * 52910, calculated for His-tagged protein, 2 * 48460, calculated for native protein, 2 * 46000, SDS-PAGE of His-tagged protein
48460
-
2 * 52910, calculated for His-tagged protein, 2 * 48460, calculated for native protein, 2 * 46000, SDS-PAGE of His-tagged protein
52910
-
2 * 52910, calculated for His-tagged protein, 2 * 48460, calculated for native protein, 2 * 46000, SDS-PAGE of His-tagged protein
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
dimer
-
2 * 52910, calculated for His-tagged protein, 2 * 48460, calculated for native protein, 2 * 46000, SDS-PAGE of His-tagged protein
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
-
complete loss of activity within 30 min. Fe2+, L-Ser D-Ser or ethanolamine decrease the loss of activity at 37°C
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
it is absolutely critical that dilutions of the purified enzyme be made in buffer containing 50% glycerol, otherwise the enzyme rapidly loses activity
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
unstable within the cell in the presence of its inducers, Gly and Leu, but not in their absence
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
anaerobic purification of His-tagged enzyme, purified protein is brown in colour
-
use of gene fusion of the structural gene sdaA to purify L-serine deaminase 1
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
-
loss of serine deaminase activity results in a hypercolonization phenotype, hypercolonization plays a role in urinary tract infections
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Newman, E.B.; Kapoor, V.
In vitro studies on L-serine deaminase activity of Escherichia coli K12
Can. J. Biochem.
58
1292-1297
1980
Escherichia coli
Isenberg, S.; Newman, E.B.
Studies on L-serine deaminase in Escherichia coli K-12
J. Bacteriol.
118
53-58
1974
Escherichia coli
Grabowski, R.; Hofmeister, A.E.M.; Buckel, W.
Bacterial L-serine dehydratases: a new family of enzymes containing iron-sulfur clusters
Trends Biochem. Sci.
18
297-300
1993
Klebsiella aerogenes, Arthrobacter globiformis, Burkholderia cepacia, Clostridium acidi-urici, Escherichia coli, Limosilactobacillus fermentum, Peptoniphilus asaccharolyticus
Su, H.; Moniakis, J.; Newman, E.B.
Use of gene fusion of the structural gene sdaA to purify L-serine deaminase 1 from Escherichia coli K-12
Eur. J. Biochem.
211
521-527
1993
Escherichia coli
Newman, E.B.; Walker, C.; Ziegler-Skylakis, K.
A possible mechanism for the in vitro activation of L-serine deaminase activity in Escherichia coli K12
Biochem. Cell Biol.
68
723-728
1990
Escherichia coli
Burman, J.D.; Harris, R.L.; Hauton, K.A.; Lawson, D.M.; Sawers, R.G.
The iron-sulfur cluster in the L-serine dehydratase TdcG from Escherichia coli is required for enzyme activity
FEBS Lett.
576
442-444
2004
Escherichia coli
Cicchillo, R.M.; Baker, M.A.; Schnitzer, E.J.; Newman, E.B.; Krebs, C.; Booker, S.J.
Escherichia coli L-serine deaminase requires a [4Fe-4S] cluster in catalysis
J. Biol. Chem.
279
32418-32425
2004
Escherichia coli
Anfora, A.T.; Haugen, B.J.; Roesch, P.; Redford, P.; Welch, R.A.
Roles of serine accumulation and catabolism in the colonization of the murine urinary tract by Escherichia coli CFT073
Infect. Immun.
75
5298-5304
2007
Escherichia coli
Zhang, X.; El-Hajj, Z.W.; Newman, E.
Deficiency in L-serine deaminase interferes with one-carbon metabolism and cell wall synthesis in Escherichia coli K-12
J. Bacteriol.
192
5515-5525
2010
Escherichia coli (P16095), Escherichia coli (P30744), Escherichia coli (P42630), Escherichia coli
EXTERNAL LINKS (specific for EC-Number 4.3.1.17)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
