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

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 4.3.2.2 - adenylosuccinate lyase and Organism(s) Escherichia coli and UniProt Accession P0AB89

for references in articles please use BRENDA:EC4.3.2.2
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
     4 Lyases
         4.3 Carbon-nitrogen lyases
             4.3.2 Amidine-lyases
                4.3.2.2 adenylosuccinate lyase
IUBMB Comments
Also acts on 1-(5-phosphoribosyl)-4-(N-succinocarboxamide)-5-aminoimidazole.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Escherichia coli
UNIPROT: P0AB89
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Escherichia coli
The enzyme appears in selected viruses and cellular organisms
Synonyms
adenylosuccinate lyase, asase, adenylosuccinase, succino-amp lyase, amps lyase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
adenylosuccinate lyase
-
adenylosuccinase
-
-
-
-
AMPS lyase
-
-
-
-
ASASE
-
-
-
-
Glutamyl-tRNA synthetase regulatory factor
-
-
-
-
lyase, adenylosuccinate
-
-
-
-
succino AMP-lyase
-
-
-
-
succino-AMP lyase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
beta-elimination
-
SYSTEMATIC NAME
IUBMB Comments
N6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming)
Also acts on 1-(5-phosphoribosyl)-4-(N-succinocarboxamide)-5-aminoimidazole.
CAS REGISTRY NUMBER
COMMENTARY hide
9027-81-0
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
fumarate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
show the reaction diagram
-
-
-
?
5-aminoimidazole-(N-succinylocarboxamide) ribotide
5-aminoimidazole-4-carboxamide ribotide + fumarate
show the reaction diagram
-
-
-
?
adenylosuccinate
AMP + fumarate
show the reaction diagram
-
-
-
?
N6-(1,2-dicarboxyethyl)AMP
fumarate + AMP
show the reaction diagram
-
-
-
?
5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide
5-aminoimidazole-4-carboxamide ribonucleotide + fumarate
show the reaction diagram
-
-
-
?
succinyladenosine monophosphate
AMP + fumarate
show the reaction diagram
-
-
-
?
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
(S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
fumarate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
show the reaction diagram
-
-
-
?
N6-(1,2-dicarboxyethyl)AMP
fumarate + AMP
show the reaction diagram
-
-
-
?
5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide
5-aminoimidazole-4-carboxamide ribonucleotide + fumarate
show the reaction diagram
-
-
-
?
succinyladenosine monophosphate
AMP + fumarate
show the reaction diagram
-
-
-
?
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.004
mutant S295A, pH 7.0
0.008
mutant H171N, pH 7.0
0.009
mutant H171A, pH 7.0
0.031
mutant H171A, pH 8.5
0.04
mutant H171N, pH 8.5
16.47
wild-type protein, pH 8.5
4.65
wild-type protein, pH 7.0
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
activity assay
8.5
activity assay
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
activity assay
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
Uniprot
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
200000
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homotetramer
-
homotetramer
x-ray crystallography
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
the crystal structures of wild-type ADL, and mutant-substrate, H171A-ADS, and -product, H171N-AMP-FUM, complexes are determined to 2.0, 1.85, and 2.0 A resolution, respectively
hanging drop vapor diffusion method, using 1.4 M sodium/potassium phosphate pH 7.5 and 4% (v/v) glycerol
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H171A
mutant to map out the residues involved in adenylosuccinate binding, and to identify the putative catalytic groups
H171N
mutant to map out the residues involved in adenylosuccinate binding, and to identify the putative catalytic groups
S295A
mutant to probe the role of S295 in the catalytic mechanism
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
using a Ni-NTA column
Q-Sepharose column chromatography and gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
subcloned from the pUC118 into the pET28a vector for expression in Escherichia coli B834DE3 cells
expressed in Escherichia coli BL21(DE3) cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Tsai, M.; Koo, J.; Yip, P.; Colman, R.F.; Segall, M.L.; Howell, P.L.
Substrate and product complexes of Escherichia coli adenylosuccinate lyase provide new insights into the enzymatic mechanism
J. Mol. Biol.
370
541-554
2007
Escherichia coli (P0AB89), Escherichia coli
Manually annotated by BRENDA team
Kozlov, G.; Nguyen, L.; Pearsall, J.; Gehring, K.
The structure of phosphate-bound Escherichia coli adenylosuccinate lyase identifies His171 as a catalytic acid
Acta Crystallogr. Sect. F
65
857-861
2009
Escherichia coli (Q8X737), Escherichia coli
Manually annotated by BRENDA team