Information on EC 4.3.2.1 - argininosuccinate lyase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea

EC NUMBER
COMMENTARY
4.3.2.1
-
RECOMMENDED NAME
GeneOntology No.
argininosuccinate lyase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2-(Nomega-L-arginino)succinate = fumarate + L-arginine
show the reaction diagram
5 residues are essential for catalytic activity: R115, N116, T161, S283, and E296
-
2-(Nomega-L-arginino)succinate = fumarate + L-arginine
show the reaction diagram
random mechanism with the formation of two dead-end complexes: enzyme-argininosuccinate-fumarate and enzyme-argininosuccinate-arginine
-
2-(Nomega-L-arginino)succinate = fumarate + L-arginine
show the reaction diagram
stepwise E1cB mechanism, rate-limiting step probably at the C-N bond-cleavage step
-
2-(Nomega-L-arginino)succinate = fumarate + L-arginine
show the reaction diagram
random uni-bi kinetic mechanism
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
elimination
-
-
elimination
-
-
elimination
Q9P870
-
elimination
-
-
C-N bond cleavage
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Alanine, aspartate and glutamate metabolism
-
-
Arginine and proline metabolism
-
-
arginine metabolism
-
-
Biosynthesis of antibiotics
-
-
Biosynthesis of secondary metabolites
-
-
canavanine biosynthesis
-
-
L-arginine biosynthesis I (via L-ornithine)
-
-
L-arginine biosynthesis II (acetyl cycle)
-
-
L-arginine biosynthesis III (via N-acetyl-L-citrulline)
-
-
L-arginine biosynthesis IV (archaebacteria)
-
-
L-citrulline-nitric oxide cycle
-
-
Metabolic pathways
-
-
urea cycle
-
-
urea cycle
-
-
SYSTEMATIC NAME
IUBMB Comments
2-(Nomega-L-arginino)succinate arginine-lyase (fumarate-forming)
-
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ARG4
-
gene name
arginine-succinate lyase
-
-
-
-
argininosuccinase
-
-
-
-
argininosuccinase
-
-
argininosuccinase
Sulfolobus solfataricus P1
-
-
-
Argininosuccinate lyase
-
-
-
-
Argininosuccinate lyase
Q9P870
-
Argininosuccinate lyase
-
-
Argininosuccinate lyase
-
-
Argininosuccinate lyase
-
-
Argininosuccinate lyase
-
-
Argininosuccinate lyase
-
-
Argininosuccinate lyase
-
-
argininosuccinic acid lyase
-
-
-
-
Arginosuccinase
-
-
-
-
ASAL
-
-
-
-
ASL
-
-
-
-
ASL
Q9P870
-
ASL
Q9P8B5
-
ASL
-
delta2-crystallin
ASL
Mus musculus BALB/c
-
-
-
ASL
Q9LAE5
-
ASL
-
-
delta2 crystallin
-
-
delta2-crystallin
-
-
-
-
hASL
-
gene name
L-argininosuccinate arginine-lyase
-
-
-
-
lyase, argininosuccinate
-
-
-
-
Rv1659
P9WPY7
gene name
Rv1659
P9WPY7
gene name
-
CAS REGISTRY NUMBER
COMMENTARY
9027-34-3
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
fragment
UniProt
Manually annotated by BRENDA team
5 major isoform of the enzyme
-
-
Manually annotated by BRENDA team
multiple forms
-
-
Manually annotated by BRENDA team
wild type and mutant enzymes: S114A, R113N, S284A, Y323F, E296Q, r115N, N116L, T161V, S283A, and Y323I
-
-
Manually annotated by BRENDA team
ASL deficiency results in the autosomal, recessive disorder argininosuccinic aciduria
-
-
Manually annotated by BRENDA team
mutations in ASL result in the clinical condition argininosuccinic aciduria, an autosomal recessive disorder
-
-
Manually annotated by BRENDA team
mutations in ASL result the clinical condition argininosuccinate aciuria
-
-
Manually annotated by BRENDA team
subspecies Lactobacillus plantarum plantarum
-
-
Manually annotated by BRENDA team
gene asl
-
-
Manually annotated by BRENDA team
Mus musculus BALB/c
gene asl
-
-
Manually annotated by BRENDA team
strain PCC 73102
SwissProt
Manually annotated by BRENDA team
Gulf toadfish
-
-
Manually annotated by BRENDA team
cv. Nipponbare, gene OsASL1
-
-
Manually annotated by BRENDA team
fawn-hooded hypertensive (FHH) rats
-
-
Manually annotated by BRENDA team
male wistar rat
-
-
Manually annotated by BRENDA team
Sulfolobus solfataricus P1
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
a point mutation of a gene encoding argininosuccinate lyase causes a short root phenotype in the root elongation defect 1 mutant ref1, the enzyme activity is lost by the mutation R140L in OsASL1.1. The mutant has a shorter length from the quiescent center to the starting point of the elongation zone but a similar cell size and number of lateral and crown roots, and similar radial structure and nutrient uptake patterns compared to the wild-type. The mutant phenotype can be rescued by exogenous addition of arginine, but not by other amino acids
malfunction
-
an increase in aspartate- and citrulline-derived argininosuccinate is a consequence of enzyme inhibition by high levels of fumarate in fumarate hydratase-deficient cells. In these cells, argininosuccinate is not produced from citrulline and aspartate in FH-deficient cells but rather from arginine and fumarate
malfunction
-
argininosuccinate aciduria is observed in patients deficient in the enzyme. An increase in aspartate- and citrulline-derived argininosuccinate is a consequence of enzyme inhibition by high levels of fumarate in fumarate hydratase-deficient cells. In these cells, argininosuccinate is not produced from citrulline and aspartate in FH-deficient cells but rather from arginine and fumarate
malfunction
-
argininosuccinic aciduria, ASA, MIM 207900, is the second most common human urea cycle disorder and is caused by deficiency of argininosuccinate lyase. Subjects with ASA disease cannot generate arginine from citrulline. Loss of the enzyme also leads to reduced NO synthesis due to decreased endogenous arginine synthesis as well as reduced utilization of extracellular arginine for NO production in humans
malfunction
-
loss of enterocyte-derived enzyme results in increased incidence of necrotizing enterocolitis, phenotype, overview
malfunction
-
loss of the enzyme leads to reduced NO synthesis due to decreased endogenous arginine synthesis as well as reduced utilization of extracellular arginine for NO production in mice. Enzyme hypomorphic mice show global NO deficiency and evidence of multi-organ dysfunction, phenotypes, hypomorphic mouse model of enzyme deficiency, overview
metabolism
-
ASL synthesizes the second step in production of arginine, which is a part of the congenital urea cycle
metabolism
-
biological activity in liver, ileum, small intestine, heart, lung and kidney within the urea and nitric oxide cycle
metabolism
-
synthesizes the second last step in the conversion of ammonia into urea
metabolism
-
small heat shock protein, alphaA-crystallin, functions as a molecular chaperone, and enhances thermal stability of both delta-crystallin and ASL. Thermal unfolding of delta-crystallin or ASL in the presence of alphaA-crystallin follows a similar three-state model. A stable intermediate which retains about 30% alpha-helical structure is observed. Protection from thermal denaturation by alphaA-crystallin is by interaction with partly unfolded ASL to form high molecular weight heteroligomers. Aggregate formation of ASL is significantly reduced in the presence of alphaA-crystallin. The extent of protection of ASL at different ratios of alpahA-crystallin is described by hyperbolic curves, suggesting the preferential recognition of partly unfolded ASL by alphaA-crystallin
metabolism
-
Sulfolobus solfataricus lacks ornithine acetyltransferase and thus forms N-acetylglutamate exclusively via the energetically less favourable reaction catalysed by N-acetylglutamate synthase, investing 1 mol of acetyl CoA per mol of N-acetyl intermediate synthesized
metabolism
P9WPY7
last enzyme in the arginine biosynthesis pathway
metabolism
-
the enzyme catalyzes the last step of arginine biosynthesis
metabolism
-
last enzyme in the arginine biosynthesis pathway
-
physiological function
-
argininosuccinate lyase in enterocytes protects from development of necrotizing enterocolitis, cell-autonomous role of the enzyme. The enzyme is required to maintain a NO synthesis complex containing NO synthase, argininosuccinate synthase, HSP90, and the arginine transporter SLC7A1
physiological function
-
loss of function of fumarate hydratase, the mitochondrial tumor suppressor and tricarboxylic acid cycle enzyme, is associated with a highly malignant form of papillary and collecting duct renal cell cancer. The accumulation of fumarate leads to reversed argininosuccinate lyase activity in fumarate hydratase-deficient cancer cells from Fh1-deficient humans, making these cells auxotrophic for arginine, which opens a therapeutic perspective for the cure of hereditary leiomyomatosis and renal cell cancer. The urea cycle metabolite argininosuccinate is a common metabolic biomarker of FH deficiency
physiological function
-
loss of function of fumarate hydratase, the mitochondrial tumor suppressor and tricarboxylic acid cycle enzyme, is associated with a highly malignant form of papillary and collecting duct renal cell cancer. The accumulation of fumarate leads to reversed argininosuccinate lyase activity in fumarate hydratase-deficient cancer cells from Fh1-deficient mice, making these cells auxotrophic for arginine
physiological function
-
the asl gene plays an important role in the replication of Brucella abortus in RAW-264.7 cells
physiological function
-
the enzyme has a structural function in addition to its catalytic activity. The enzyme plays a more central role in cellular arginine utilization for NO synthesis beyond intracellular recycling of citrulline into arginine
physiological function
-
the enzyme is required for arginine production for use in normal root elongation in rice
physiological function
Mus musculus BALB/c
-
the asl gene plays an important role in the replication of Brucella abortus in RAW-264.7 cells
-
metabolism
Sulfolobus solfataricus P1
-
Sulfolobus solfataricus lacks ornithine acetyltransferase and thus forms N-acetylglutamate exclusively via the energetically less favourable reaction catalysed by N-acetylglutamate synthase, investing 1 mol of acetyl CoA per mol of N-acetyl intermediate synthesized
-
additional information
-
Asl enzyme-dependent nitric oxide synthase complex
additional information
-
depleting arginine from the growth media by the addition of pegylated arginine deiminase decreases the production of argininosuccinate in FH-deficient cells and reduces cell survival and proliferation
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(Nomega-L-arginino)succinate
fumarate + L-arginine
show the reaction diagram
-
-
-
?
(Nomega-L-arginino)succinate
fumarate + L-arginine
show the reaction diagram
-
-
-
?
(Nomega-L-arginino)succinate
fumarate + L-arginine
show the reaction diagram
-
-
-
?
(Nomega-L-arginino)succinate
fumarate + L-arginine
show the reaction diagram
-
-
-
?
(Nomega-L-arginino)succinate
fumarate + L-arginine
show the reaction diagram
-
-
-
-
?
(Nomega-L-arginino)succinate
fumarate + L-arginine
show the reaction diagram
-
-
-
r
(Nomega-L-arginino)succinate
fumarate + L-arginine
show the reaction diagram
-
-
-
r
(Nomega-L-arginino)succinate
fumarate + L-arginine
show the reaction diagram
-
-
-
r
(Nomega-L-arginino)succinate
fumarate + L-arginine
show the reaction diagram
-
-
-
r
(Nomega-L-arginino)succinate
fumarate + L-arginine
show the reaction diagram
-
-
-
?
(Nomega-L-arginino)succinate
fumarate + L-arginine
show the reaction diagram
-
-
-
?
(Nomega-L-arginino)succinate
fumarate + L-arginine
show the reaction diagram
-
-
-
?
(Nomega-L-arginino)succinate
fumarate + L-arginine
show the reaction diagram
-
-
-
r
(Nomega-L-arginino)succinate
fumarate + L-arginine
show the reaction diagram
-
-
-
r
(Nomega-L-arginino)succinate
fumarate + L-arginine
show the reaction diagram
-
-
-
r
(Nomega-L-arginino)succinate
fumarate + L-arginine
show the reaction diagram
-
-
-
?, r
(Nomega-L-arginino)succinate
fumarate + L-arginine
show the reaction diagram
-
-
-
?, r
(Nomega-L-arginino)succinate
fumarate + L-arginine
show the reaction diagram
-
-
-
?
(Nomega-L-arginino)succinate
fumarate + L-arginine
show the reaction diagram
Q9LAE5
-
-
?
(Nomega-L-arginino)succinate
fumarate + L-arginine
show the reaction diagram
Q9LAE5
-
-
r
(Nomega-L-arginino)succinate
fumarate + L-arginine
show the reaction diagram
-
last step in the biosynthesis of arginine
-
r
2-(Nomega-L-arginino)succinate
fumarate + L-arginine
show the reaction diagram
-
-
-
-
r
2-(Nomega-L-arginino)succinate
fumarate + L-arginine
show the reaction diagram
-
-
-
-
r
2-(Nomega-L-arginino)succinate
fumarate + L-arginine
show the reaction diagram
-
-
-
-
?
2-(Nomega-L-arginino)succinate
fumarate + L-arginine
show the reaction diagram
-
-
-
-
r
2-(Nomega-L-arginino)succinate
fumarate + L-arginine
show the reaction diagram
Q9P870
-
-
-
?
arginine + fumarate
argininosuccinate
show the reaction diagram
-
-
-
-
y
argininosuccinate
fumarate + L-Arg
show the reaction diagram
-
-
-
?
argininosuccinate
fumarate + L-Arg
show the reaction diagram
-
-
-
?
argininosuccinate
fumarate + L-Arg
show the reaction diagram
-
-
-
?
argininosuccinate
fumarate + L-Arg
show the reaction diagram
-
-
-
?
argininosuccinate
fumarate + L-Arg
show the reaction diagram
-
-
-
?
argininosuccinate
fumarate + L-Arg
show the reaction diagram
-
-
-
?
argininosuccinate
fumarate + L-Arg
show the reaction diagram
-
-
-
-
?
argininosuccinate
fumarate + L-Arg
show the reaction diagram
-
-
-
r
argininosuccinate
fumarate + L-Arg
show the reaction diagram
-
-
-
-
r
argininosuccinate
fumarate + L-Arg
show the reaction diagram
-
-
-
-
argininosuccinate
fumarate + L-Arg
show the reaction diagram
-
-
-
?
argininosuccinate
fumarate + L-Arg
show the reaction diagram
-
-
-
?
argininosuccinate
fumarate + L-Arg
show the reaction diagram
-
-
-
?
argininosuccinate
fumarate + L-Arg
show the reaction diagram
-
-
-
?
argininosuccinate
fumarate + L-Arg
show the reaction diagram
-
-
-
?
argininosuccinate
fumarate + L-Arg
show the reaction diagram
-
-
-
?
argininosuccinate
fumarate + L-Arg
show the reaction diagram
-
-
-
?
argininosuccinate
fumarate + L-Arg
show the reaction diagram
-
-
-
?
argininosuccinate
fumarate + L-Arg
show the reaction diagram
-
-
-
?
argininosuccinate
fumarate + L-Arg
show the reaction diagram
-
-
-
?
argininosuccinate
fumarate + L-Arg
show the reaction diagram
-
-
-
r
argininosuccinate
fumarate + L-Arg
show the reaction diagram
-
-
-
r
argininosuccinate
fumarate + L-Arg
show the reaction diagram
-
-
-
-
?
argininosuccinate
fumarate + L-Arg
show the reaction diagram
-
-
-
-
?
argininosuccinate
fumarate + L-Arg
show the reaction diagram
-
-
-
-
argininosuccinate
fumarate + L-Arg
show the reaction diagram
-
-
-
-
argininosuccinate
fumarate + L-Arg
show the reaction diagram
Q9P8B5
-
-
-
?
argininosuccinate
fumarate + L-Arg
show the reaction diagram
-
biological activity in liver, ileum, small intestine, heart, lung and kidney within the urea and nitric oxide cycle
-
-
?
argininosuccinate
?
show the reaction diagram
-
urea cycle enzyme, deficiency results in argininosuccinic aciduria
-
-
-
difluorofumarate + L-Arg
?
show the reaction diagram
-
-
-
-
?
fumarate + arginine
argininosuccinate
show the reaction diagram
-
-
-
-
r
fumarate + L-Arg
argininosuccinate
show the reaction diagram
-
-
-
r
fumarate + L-Arg
argininosuccinate
show the reaction diagram
-
-
-
r
fumarate + L-Arg
argininosuccinate
show the reaction diagram
-
-
-
r
fumarate + L-Arg
argininosuccinate
show the reaction diagram
-
-
-
r
fumarate + L-Arg
argininosuccinate
show the reaction diagram
-
-
-
r
fumarate + L-Arg
argininosuccinate
show the reaction diagram
-
-
-
-
fumarate + L-Arg
argininosuccinate
show the reaction diagram
-
-
-
r
fumarate + L-arginine
2-(Nomega-L-arginino)succinate
show the reaction diagram
-
accumulation of fumarate leads to reversed argininosuccinate lyase activity in fumarate hydratase-deficient cancer cells
-
-
r
fumarate + L-canavanine
?
show the reaction diagram
-
at 78% of the activity with L-Arg
-
-
?
omega-N-(L-arginino)succinate
L-arginine + fumarate
show the reaction diagram
-
-
-
-
?
omega-N-(L-arginino)succinate
L-arginine + fumarate
show the reaction diagram
-
-
-
-
?
omega-N-(L-arginino)succinate
L-arginine + fumarate
show the reaction diagram
-
-
-
-
?
monofluorofumarate + L-Arg
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
metabolic role in biosynthesis of Arg and urea
-
-
-
additional information
?
-
-
enzyme is involved in arginine biosynthesis and in urea cycle
-
-
-
additional information
?
-
-
the genetic variant OsASL1.1 has argininosuccinate lyase activity, while variant OsASL1.2 has no activity
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(Nomega-L-arginino)succinate
fumarate + L-arginine
show the reaction diagram
-
-
-
r
(Nomega-L-arginino)succinate
fumarate + L-arginine
show the reaction diagram
-
-
-
r
(Nomega-L-arginino)succinate
fumarate + L-arginine
show the reaction diagram
-
-
-
r
(Nomega-L-arginino)succinate
fumarate + L-arginine
show the reaction diagram
-
-
-
r
(Nomega-L-arginino)succinate
fumarate + L-arginine
show the reaction diagram
-
-
-
r
(Nomega-L-arginino)succinate
fumarate + L-arginine
show the reaction diagram
-
-
-
r
(Nomega-L-arginino)succinate
fumarate + L-arginine
show the reaction diagram
-
-
-
r
(Nomega-L-arginino)succinate
fumarate + L-arginine
show the reaction diagram
-
-
-
r
(Nomega-L-arginino)succinate
fumarate + L-arginine
show the reaction diagram
-
-
-
r
(Nomega-L-arginino)succinate
fumarate + L-arginine
show the reaction diagram
Q9LAE5
-
-
r
(Nomega-L-arginino)succinate
fumarate + L-arginine
show the reaction diagram
-
last step in the biosynthesis of arginine
-
r
2-(Nomega-L-arginino)succinate
fumarate + L-arginine
show the reaction diagram
-
-
-
-
r
2-(Nomega-L-arginino)succinate
fumarate + L-arginine
show the reaction diagram
-
-
-
-
?
2-(Nomega-L-arginino)succinate
fumarate + L-arginine
show the reaction diagram
-
-
-
-
r
2-(Nomega-L-arginino)succinate
fumarate + L-arginine
show the reaction diagram
Q9P870
-
-
-
?
argininosuccinate
fumarate + L-Arg
show the reaction diagram
-
-
-
-
?
argininosuccinate
fumarate + L-Arg
show the reaction diagram
-
-
-
-
?
argininosuccinate
fumarate + L-Arg
show the reaction diagram
-
biological activity in liver, ileum, small intestine, heart, lung and kidney within the urea and nitric oxide cycle
-
-
?
argininosuccinate
?
show the reaction diagram
-
urea cycle enzyme, deficiency results in argininosuccinic aciduria
-
-
-
omega-N-(L-arginino)succinate
L-arginine + fumarate
show the reaction diagram
-
-
-
-
?
omega-N-(L-arginino)succinate
L-arginine + fumarate
show the reaction diagram
-
-
-
-
?
omega-N-(L-arginino)succinate
L-arginine + fumarate
show the reaction diagram
-
-
-
-
?
fumarate + L-arginine
2-(Nomega-L-arginino)succinate
show the reaction diagram
-
accumulation of fumarate leads to reversed argininosuccinate lyase activity in fumarate hydratase-deficient cancer cells
-
-
r
additional information
?
-
-
metabolic role in biosynthesis of Arg and urea
-
-
-
additional information
?
-
-
enzyme is involved in arginine biosynthesis and in urea cycle
-
-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
GDP
-
0.2 mM, slight stimulation
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1-ethyl-3-(3-diethylaminopropyl)carbodiimide
-
at pH 6
acetylenedicarboxylate
-
-
Arg
-
noncompetitive versus argininosuccinate
argininosuccinate
-
0.3 mM inhibits the reaction by 97%
bromomesaconic acid
-
argininosuccinate completely protects, Lys51 has an essential role in binding of argininosuccinate and consequently is essential in catalysis; inactivation follows pseudo-first-order kinetics
citrulline
-
competitive versus Arg and noncompetitive versus argininosuccinate and fumarate
citrulline
-
noncompetitive vs. fumarate and arginine
D-glucose
-
12.5 mM glucose decreases activity of ASL by 20%, 25 mM glucose by 50%
diethyl dicarbonate
-
-
diethyl dicarbonate
-
-
diethyl dicarbonate
-
modification of an essential His
difluorofumarate
-
pseudo-first-order process
fumarate
-
noncompetitive versus argininosuccinate
N3-(L-1-carboxy-2-nitroethyl)-L-arginine
-
-
succinate
-
dead-end inhibitor
succinate
-
noncompetitive vs. fumarate and arginine
Urea
-
competitive
monofluorofumarate
-
reversible, pseudo-first-order process
additional information
-
the antibody of the liver enzyme is an effective inhibitor of brain enzyme
-
additional information
-
mRNA expression and activity of liver argininosuccinate lyase decrease with age
-
additional information
-
acetylation at Lys288 or Lys69 decreases activity of ASL
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
amino acids
-
extra amino acids in culture media increases activity of ASL by decreasing inhibitory acetylation rate
GTP
-
0.2 mM, stimulates
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.2
(Nomega-L-arginino)succinate
-
mutant c.532 G>A, pH 7.5, 37C
0.23
(Nomega-L-arginino)succinate
-
mutant c.1135 C>T, pH 7.5, 37C
2.6
(Nomega-L-arginino)succinate
-
wild-type, pH 7.5, 37C
3
Arg
-
-
3
arginine
-
-
0.007
argininosuccinate
-
delta-crystallin IVa
0.008
argininosuccinate
-
delta-crystallin IIIa
0.016
argininosuccinate
-
delta-crystallin Ia and delta-crystallin IIa
0.02
argininosuccinate
-
mutant enzyme S284A
0.022
argininosuccinate
-
-
0.024
argininosuccinate
-
delta-crystallin IVb
0.029
argininosuccinate
-
-
0.03
argininosuccinate
-
mutant enzyme R113N
0.031
argininosuccinate
-
delta-crystallin IIIb
0.037
argininosuccinate
-
Km-value at low concentrations of argininosuccinate
0.039
argininosuccinate
-
delta-crystallin VIb
0.042
argininosuccinate
-
delta-crystallin Vb
0.044
argininosuccinate
-
delta-crystallin VIIb
0.05
argininosuccinate
-
delta-crystallin IIb
0.07
argininosuccinate
-
wild-type enzyme
0.09
argininosuccinate
-
mutant enzyme S114A
0.1
argininosuccinate
-
-
0.1
argininosuccinate
-
enzyme form deltaB
0.13
argininosuccinate
-
enzyme form deltaC
0.144
argininosuccinate
-
31C
0.146
argininosuccinate
-
26C
0.151
argininosuccinate
-
21C
0.16
argininosuccinate
-
Km-value at high concentrations of argininosuccinate
0.183
argininosuccinate
-
enzyme form deltaD
0.187
argininosuccinate
-
enzyme form deltaE
0.2
argininosuccinate
-
-
0.26
argininosuccinate
-
pH 7.5, 37C
0.35
argininosuccinate
-
-
0.4
argininosuccinate
-
-
1.7
argininosuccinate
-
mutant enzyme Y323F
0.046
difluorofumarate
-
-
0.045
disodium argininosuccinate
-
wild type, 25 C, 10 mM Tris-HCl, pH 7.5, 1 mM EDTA
0.069
disodium argininosuccinate
-
mutant W9R, 25 C, 10 mM Tris-HCl, pH 7.5, 1 mM EDTA
0.083
disodium argininosuccinate
-
mutant TRUN1-8, 25 C, 10 mM Tris-HCl, pH 7.5, 1 mM EDTA
0.105
disodium argininosuccinate
-
mutant TRUN1-9, 25 C, 10 mM Tris-HCl, pH 7.5, 1 mM EDTA
0.106
disodium argininosuccinate
-
mutant W9Y, 25 C, 10 mM Tris-HCl, pH 7.5, 1 mM EDTA
0.111
disodium argininosuccinate
-
mutant W9F, 25 C, 10 mM Tris-HCl, pH 7.5, 1 mM EDTA
0.112
disodium argininosuccinate
-
mutant W9A, 25 C, 10 mM Tris-HCl, pH 7.5, 1 mM EDTA
0.115
disodium argininosuccinate
-
mutant W9M, 25 C, 10 mM Tris-HCl, pH 7.5, 1 mM EDTA
0.119
disodium argininosuccinate
-
211-chimera, 25 C, 10 mM Tris-HCl, pH 7.5, 1 mM EDTA
0.212
disodium argininosuccinate
-
mutant M9F/E115D, 25 C, 10 mM Tris-HCl, pH 7.5, 1 mM EDTA
0.255
disodium argininosuccinate
-
mutant D115A, 25 C, 10 mM Tris-HCl, pH 7.5, 1 mM EDTA
0.273
disodium argininosuccinate
-
mutant D115E, 25 C, 10 mM Tris-HCl, pH 7.5, 1 mM EDTA
0.294
disodium argininosuccinate
-
mutant M9W/E115D, 25 C, 10 mM Tris-HCl, pH 7.5, 1 mM EDTA
0.61
disodium argininosuccinate
-
mutant M9Y/E115D, 25 C, 10 mM Tris-HCl, pH 7.5, 1 mM EDTA
2.724
disodium argininosuccinate
-
mutant M9W, 25 C, 10 mM Tris-HCl, pH 7.5, 1 mM EDTA
3.159
disodium argininosuccinate
-
mutant M9W/V14S, 25 C, 10 mM Tris-HCl, pH 7.5, 1 mM EDTA
0.067
fumarate
-
-
4.5
fumarate
-
-
5.3
fumarate
-
-
1.4
monofluorofumarate
-
-
additional information
additional information
-
-
-
additional information
additional information
-
Km-values of the multiple form of delta-crystallin
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.12
argininosuccinate
-
mutant enzyme S284A
0.43
argininosuccinate
-
mutant enzyme Y323F
0.62
argininosuccinate
-
mutant enzyme R113N
2.42
argininosuccinate
-
mutant enzyme S114A
3.28
argininosuccinate
-
-
4.9
argininosuccinate
-
wild-type enzyme
2500
argininosuccinate
-
-
2930
argininosuccinate
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0012
-
activity in lung homogenate
0.003
-
pH and temperature not specified in the publication, activity in cell culture in growth medium with 0.5% peptone and 0.1%yeast extract
0.003
-
pH and temperature not specified in the publication, activity in cell culture in growth medium with 0.2% yeast extract
0.006
-
pH and temperature not specified in the publication, activity in cell culture in minimal growth medium with 20 mM glucose and 5 mM NH4+
3
-
mutant c.C1153T, pH 7.5, 37C
5
-
mutant c.A943G, pH 7.5, 37C
8
-
formation of argininosuccinate
8
-
synthesis of argininosuccinate
8.6
-
pRH1, units/mg
10.3
-
cleavage of argininosuccinate
10.3
-
deamination of argininosuccinate
20
-
mutant c.T299C, pH 7.5, 37C
23
-
-
23
-
mutant c.A857G, pH 7.5, 37C
41
-
mutant c.A566G, pH 7.5, 37C
208
-
mutant c.G532A, pH 7.5, 37C
280
-
mutant c.C1135T, pH 7.5, 37C
4227
-
wild-type, pH 7.5, 37C
additional information
-
-
additional information
-
-
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.8 - 7.2
-
formation of argininosuccinate
7.4
-
activity assay
7.5
-
a plateau above pH 7.5, cleavage of argininosuccinate; a plateau below pH 7.5, formation of argininosuccinate
7.5
-
formation of argininosuccinate
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
-
activity assay
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.2
-
isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
striatal neurons
Manually annotated by BRENDA team
-
low mRNA content
Manually annotated by BRENDA team
-
present in neurones and nerve fibres in the myenteric plexus of the lower oesophagael sphincter, antrum, pylorus, ileum and colon, in the submucosal plexus of ileum and colon, in longitudinal muscle of ileum and colon, nerve bundles of circular muscles
Manually annotated by BRENDA team
-
ASL expression is time-dependently reduced in hypoxia
Manually annotated by BRENDA team
-
intestinal segments from neonatal pups
Manually annotated by BRENDA team
P04424
using DNA
Manually annotated by BRENDA team
-
predominant expression
Manually annotated by BRENDA team
-
mRNA detectable
Manually annotated by BRENDA team
-
neurons of the myenteric plexus
Manually annotated by BRENDA team
Mus musculus BALB/c
-
-
-
Manually annotated by BRENDA team
-
expression of enzyme genetic variant OsASL1.1
Manually annotated by BRENDA team
-
expression of enzyme genetic variant OsASL1.1
Manually annotated by BRENDA team
-
low mRNA content
Manually annotated by BRENDA team
-
nerve fibers of smooth muscle layer
Manually annotated by BRENDA team
-
fumarate hydratase defiecient or proficient cells, the latter termed UOKpFH cells
Manually annotated by BRENDA team
additional information
-
not found in oligodendrocytes
Manually annotated by BRENDA team
additional information
-
expression patterns of OsASL1.1 and OsALS1.2, abundance of OsALS1.2 is much lower than that of OsASL1.1 in either tissue, overview
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
expression of OsASL1.1
Manually annotated by BRENDA team
-
expression of OsASL1.1
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50000
-
SDS-PAGE
710057
51700
-
SDS-PAGE
699983
52340
Q9P870
the asl open reading frame encodes a protein of 464 amino acids with a calculated mass of 52337 Da
676120
187000
-
equilibrium sedimentation
34429
190000
-
disc gel electrophoresis
34431
190000
-
gel filtration
34442
200000
-
gel filtration
34428
200000
-
-
34431
202000
-
gel filtration
34430
215000
Q9LAE5
native PAGE, recombinant ASL
650920
218000
-
gel filtration
34422
220000
Q8DVX5
gel filtration, recombinant fusion protein
713670
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
4 * 50000, SDS-PAGE
?
-
x * 55000, SDS-PAGE
?
-
x * 51663, calculation from nucleotide sequence
?
-
x * 51944, calculation from nucleotide sequence
hexamer
-
5 or 6 * 39000, SDS-PAGE
homotetramer
-
-
homotetramer
P9WPY7
4 * 50900, recombinant His-tagged enzyme, SDS-PAGE
pentamer
-
5 or 6 * 39000, SDS-PAGE
tetramer
-
-
tetramer
-
4 * 50000, SDS-PAGE
tetramer
-
4 * 50000, SDS-PAGE
tetramer
-
4 * 50000, SDS-PAGE
tetramer
-
4 * 49000, SDS-PAGE
tetramer
-
4 * 50400, equilibrium sedimentation in presence of urea and guanidine hydrochloride
tetramer
-
4 * 51600, deduced from nucleotide sequence
tetramer
Q9LAE5
4 * 53000, SDS-PAGe, recombinant ASL
tetramer
Q8DVX5
4 * 51500, calculated
homotetramer
-
4 * 50900, recombinant His-tagged enzyme, SDS-PAGE
-
additional information
-
small heat shock protein, alphaA-crystallin, functions as a molecular chaperone, and enhances thermal stability of both delta-crystallin and ASL. Thermal unfolding of delta-crystallin or ASL in the presence of alphaA-crystallin follows a similar three-state model. A stable intermediate which retains about 30% alpha-helical structure is observed. Protection from thermal denaturation by alphaA-crystallin is by interaction with partly unfolded ASL to form high molecular weight heteroligomers. Aggregate formation of ASL is significantly reduced in the presence of alphaA-crystallin. The extent of protection of ASL at different ratios of alpahA-crystallin is described by hyperbolic curves, suggesting the preferential recognition of partly unfolded ASL by alphaA-crystallin
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
side-chain modification
-
acetylation at Lys288 or Lys69 in liver decreases activity of ASL
additional information
-
origin of the multiple forms is due to post-translational oxidative modification of the protein
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
S283A mutant, hanging-drop vapor diffusion at room temperatur, 9 mg/ml protein in 10 mM Tris-HCl, pH 7.5 and 1 mM EDTA is preincubated with 75 mM argininosuccinate, subsequently 0.005 ml drops of the solution are mixed with an equal ammount of precipitating solution consisting of 12% polyethylene glycol 2000 MME, 300 mM MgCl2, 100 mM HEPES, pH 7.4, crystals diffract to 1.96 A resolution
-
apoenzyme and complex of double loop mutant with sulfate, growing at room temperature using the hanging drop vapor diffusion method, molecular replacement at 2.2 A resolution for the DLM-sulfate complex, 2.5 A resolution for the apoenzyme
-
crystallized from a highly concentrated sample of purified recombinant alpha-methylacyl-CoA-racemase with arginosuccinate lyase as a minor impurity, growing at room temperature in mother liquid consisting of 1.26 M ammonium phosphate pH 7.0, small bipyramidal crystals, molecular replacement at 2.44 A resolution
-
hanging-drop vapor diffusion, crystal structure of Q286R mutant at 2.65 A
-
purified recombinant His-tagged enzyme, microbatch-under-oil method, mixing of 0.002 ml of 9.5 mg/ml protein in 25 mM phosphate buffer, pH 7.4, with 0.002 ml of precipitant solution containing 100 mM Bis-Tris, pH 5.5, 25% w/v polyethylene glycol 3350, X-ray diffraction structure determination and analysis at 2.40 A resolution, molecular replacement method
P9WPY7
to 2.5 A resolution, space group R3
Q8DVX5
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5 - 8.5
-
stable for at least 20 min
34436
7
-
at 4C and at 25C, 8 h, stable
34429
8.2
-
25C, about 40% loss of activity after 8 h; 4C, about 60% loss of activity after 4 h
34429
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4
-
Tris-HCl buffer, pH 8.5, 50% loss of activity after 2.3 h
34428
38
-
30 min, stable
34428
49
-
20 min, 50% inactivation
34443
52
-
20 min, 50% inactivation
34443
54
-
mid-point temperature transition 2
714375
57
-
mid-point temperature transition 1 and 3
714375
58
-
mid-point temperature transition 3, presence of alphaA-crystallin
714375
60
-
-
34443
60
-
20 min, 50% inactivation
34443
60
-
30 min, enzyme form deltaIIb and deltaIVb are stable
34445
65
-
complete denaturation
34437
83
-
mid-point temperature transition 1, presence of alphaA-crystallin
714375
85
-
mid-point temperature transition 2, presence of alphaA-crystallin
714375
additional information
-
enzyme forms with higher isoelectric point are much more thermostable than those with lower pI values
34445
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
Arg or phosphate ions protect from cold inactivation
-
phosphate, arsenate, 20% dimethylsulfoxide or 20% glycerol protects against cold inactivation
-
ASL undergoes cold dissociation via a dimer intermediate
-
repeated freezing and thawing does not appreciably alter the activity
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
0C, Tris buffer, pH 8.5, 50% loss of activity after 2.5 h
-
4C, Tris-HCl buffer, pH 8.5, 50% loss of activity after 2.3 h
-
frozen in 0.1 M potassium phosphate, pH 7.0, stable
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged ASL
-
leaf extract is centrifuged, the supernatant lyophilized, the resuspended material is partially purified on a G-15 Sephadex and a Q-Sepharose FF column
-
brain
-
kidney
-
liver ASL
-
recombinant ASL
-
recombinant C-terminally His-tagged enzyme from Escherichia coli strain BL21 (DE3) by nickel affinity chromatography and dialysis to homogeneity
P9WPY7
recombinant His-tagged ASL
Q9LAE5
recombinant protein
Q8DVX5
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
into the pGEM-T vector for sequence analysis
Q9P870
expression in Escherichia coli
-
expression in Saccharomyces cerevisiae and in Escherichia coli
-
expressed as His tag enzyme
-
expressed as His tag enzymes
-
expression in Escherichia coli argH auxotroph, deficient in argininosuccinate lyase
-
expression in mouse cells
-
cloning of cDNA
-
expression in Escherichia coli
-
expression in Escherichia coli and COS-7 cells
-
in vitro overexpression of ASL enzyme mutant R236W in COS7 cells andprimary fibroblasts
-
overexpressed in HEK293T cells or in Escherichia coli
-
cloning of argH gene encoding ASL
-
gene asl, quantitative realtime PCR expression analysis in infected and control cells
-
gene argH, expression of Rv1659 as His-tagged protein, with an extra methionine at the N-terminus and an extended sequence LEHHHHHH at the C-terminus, in Escherichia coli strain BL21 (DE3)
P9WPY7
expression in Escherichia coli
Q9LAE5
gene OsASL1, two variants OsASL1.1 and OsASL1.2 resulting from different transcription start sites, map-based cloning, only OsASL1.1 is able to complement the ref1 mutant phenotype, functional expression of OsASL1.1 in Saccharomyces cerevisiae, plastid-localized expression of OsASL1.1-GFP fusion protein in onion epidermal cells
-
expression in Escherichia coli
Q8DVX5
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
Brucella abortus strain 2308 infection highly induces enzyme expression in RAW-264.7 cells
-
Brucella abortus strain 2308 infection highly induces enzyme expression in RAW-264.7 cells
Mus musculus BALB/c
-
-
mRNA levels in liver decrease significantly when gulf toadfishes are crowded by 7 days
-
expression of ASL is significantly decreased to 50% in Shunt lambs
-
threefold repression of enzyme formation by arginine
-
threefold repression of enzyme formation by arginine
Sulfolobus solfataricus P1
-
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E296Q
-
retains only 0.001% residual activity
N116L
-
no activity
R115N
-
no activity
S283A
-
no activity
S384A
-
catalytic efficiency is decreased by an order of magnitude in comparison to wild-type delta II crystallin
T161V
-
no activity
Y323F
-
catalytic efficiency is decreased by an order of magnitude in comparison to wild-type delta II crystallin
Y323I
-
no activity
A41G/I43M
-
mutant without enzyme activity
D115A
-
mutant with 45% enzyme activity
D115E
-
mutant with 42.6% enzyme activity
E115D
-
mutant without enzyme activity
I143M
-
mutant without enzyme activity
M9F/E115D
-
mutant with 3.3% enzyme activity
M9W
-
mutant with 2.0% enzyme activity
M9W/E115D
-
mutant with 17% enzyme activity
M9W/V14S
-
mutant with 1.9% enzyme activity
TRUN1-8
-
mutant with 37% enzyme activity
TRUN1-9
-
mutant with 2.1% enzyme activity
W9A
-
mutant with 1.9% enzyme activity
W9F
-
mutant with 11.3% enzyme activity
W9M
-
mutant with 1.0% enzyme activity
W9R
-
mutant with 3% enzyme activity
W9Y
-
mutant with 49.5% enzyme activity
A398D
-
no activity, 15.55 of wild-type activity if coexpressed with Q286R
D31N
P04424
missense mutation found in patients with late onset of argininosuccinic aciduria, residual activity
D87G
-
no activity, 35.2% of wild-type activity if coexpressed with Q286R
E73K
P04424
missense mutation found in patient with neonatal onset of argininosuccinic aciduria, enzyme inactive
K288R
-
132% of wild-type activity
M360T
-
no actiivty, 10% of wild-type activity if coexpressed with Q286R
Q286R
-
3% of wild-type activity
Q286R
-
frequently complementing allele, 2% of wild-type kcat
Q286R
P04424
missense mutation found in patient with neonatal onset of argininosuccinic aciduria, enzyme inactive
R113Q
P04424
missense mutation found in patient with neonatal onset of argininosuccinic aciduria, enzyme inactive
R113Q
-
site-directed mutagenesis, the R113Q mutation abolishes the catalytic activity of the enzyme without affecting its protein stability
R12Q
-
6% of wild-type kcat
R182Q
P04424
missense mutation found in patient with late onset of argininosuccinic aciduria, enzyme inactive
R186Q
P04424
missense mutation found in patient with neonatal onset of argininosuccinic aciduria, residual activity
R236W
P04424
missense mutation found in patient with neonatal onset of argininosuccinic aciduria, enzyme inactive
R236W
-
site-directed mutagenesis, catalytically inactive mutant, that is structurally intact
R297Q
P04424
missense mutation found in patient with late onset of argininosuccinic aciduria, residual activity
R456W missense mutation found in patient with neonatal onset of argininosuccinic aciduria
P04424
, residual activity
V178M
P04424
missense mutation combined with mutation R186Q on the other allele found in patient with neonatal onset of argininosuccinic aciduria, enzyme activity reduced compared to wild-type
M9Y/E115D
-
mutant with 5.5% enzyme activity
additional information
-
double loop mutant DLM, enzymatically inactive
M382R
P04424
missense mutation found in patient with neonatal onset of argininosuccinic aciduria, residual activity
additional information
-
the mutations E86A and R113W identified on separate alleles are most likely to determine ASL-deficiency in a severely affected patient with neonatal onset of the disease
additional information
-
expression of mutant ASL proteins in Escherichia coli. The known classical p.Q286R, the novel classical p.K315E and the known mutations p.I100T, p.E189G and p.R385C, which all have been linked to a mild phenotype of argininosuccinic aciduria, show no significant residual activity. There is some enzyme activity detected with the p.V178M (5% of wild-type), and p.R379C (10% of wild-type) mutations in which Km values for argininosuccinic acid differs significantly from the wild-type ASL protein
V335L
P04424
missense mutation found in patients with late onset of argininosuccinic aciduria, enzyme activity reduced compared to wild-type
additional information
-
construction of an asl gene-deleted mutant strain S2308DELTAASL by allelic exchange involving insertion of a chloramphenicol resistance cassette in a BamHI site
additional information
-
generation of enterocyte-specific knockout mice of the enzyme Asl by intercrossing Aslflox/flox mice with transgenic mice expressing Cre recombinase under the control of the villin promoter. Emgineered mice are grossly indistinguishable from their littermate Aslflox/flox controls and exhibit similar growth curves and life span. Enterocytes isolated from mutant mice demonstrate an 80% reduction in mRNA expression of the enzyme
additional information
Mus musculus BALB/c
-
construction of an asl gene-deleted mutant strain S2308DELTAASL by allelic exchange involving insertion of a chloramphenicol resistance cassette in a BamHI site
-
additional information
-
isolation of the osred1, i.e. Oryza sativa root elongation defect, mutant from a short root-phenotype Tos-17 transposon insertion line, NE7046
R140L
-
naturally occuring mutation of variant OsASL1.1, which renders the enzyme catalytically inactive
additional information
-
knock-down of enzyme Asl in IEC-6 cells using lentivirus encoding shRNA targeting the enzyme. Loss of the enzyme impairs the migration of IEC-6 cells during conditions of stress
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
diagnostics
-
the urea cycle metabolite argininosuccinate is a common metabolic biomarker of FH deficiency
medicine
-
argininosuccinate lyase is a valuable marker for estimating hepatopathy
medicine
-
expression of mutant ASL proteins in Escherichia coli. The known classical p.Q286R, the novel classical p.K315E and the known mutations p.I100T, p.E189G and p.R385C, which all have been linked to a mild phenotype of argininosuccinic aciduria, show no significant residual activity. There is some enzyme activity detected with the p.V178M (5% of wild-type), and p.R379C (10% of wild-type) mutations in which Km values for argininosuccinic acid differs significantly from the wild-type ASL protein
medicine
-
loss of function of fumarate hydratase, the mitochondrial tumor suppressor and tricarboxylic acid cycle enzyme, is associated with a highly malignant form of papillary and collecting duct renal cell cancer The accumulation of fumarate leads to reversed argininosuccinate lyase activity in fumarate hydratase-deficient cancer cells from Fh1-deficient humans, making these cells auxotrophic for arginine, which opens a therapeutic perspective for the cure of hereditary leiomyomatosis and renal cell cancer
medicine
-
the enzyme may serve as a target for manipulating NO production and treatment of NO-related diseases
diagnostics
-
the enzyme may be used as a candidate marker for serodiagnosis of brucellosis
diagnostics
-
the urea cycle metabolite argininosuccinate is a common metabolic biomarker of FH deficiency
medicine
-
manipulating the enzyme expression or activity might be of potential benefit for treatment of necrotizing enterocolitis
diagnostics
Mus musculus BALB/c
-
the enzyme may be used as a candidate marker for serodiagnosis of brucellosis
-
medicine
-
argininosuccinate lyase is present in activated microglia cells in the ischemic rat
medicine
-
transient ischemia induces changes in the number and percentage of the nNOS+ neurons also expressing argininosuccinate lyase
medicine
-
manipulating the enzyme expression or activity might be of potential benefit for treatment of necrotizing enterocolitis
analysis
-
the rapid and sensitive assay method is used to detect increases in the activity in serum from patients with liver diseases