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Literature summary extracted from

  • Crifo, C.; Siems, W.; Soro, S.; Salerno, C.
    Inhibition of defective adenylosuccinate lyase by HNE: a neurological disease that may be affected by oxidative stress (2005), Biofactors, 24, 131-136.
    View publication on PubMed

Application

EC Number Application Comment Organism
4.3.2.2 additional information participates in the purine biosynthetic pathway, enzyme defects result in psychomotor retardation, epilepsy, muscle wasting and autistic features Bacillus subtilis
4.3.2.2 additional information participates in the purine biosynthetic pathway, enzyme defects result in psychomotor retardation, epilepsy, muscle wasting and autistic features Homo sapiens
4.3.2.2 additional information participates in the purine biosynthetic pathway, enzyme defects result in psychomotor retardation, epilepsy, muscle wasting and autistic features Thermotoga maritima
4.3.2.2 additional information participates in the purine biosynthetic pathway, enzyme defects result in psychomotor retardation, epilepsy, muscle wasting and autistic features Pyrobaculum aerophilum

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.3.2.2 expression in Escherichia coli Homo sapiens

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.3.2.2
-
Bacillus subtilis
4.3.2.2
-
Thermotoga maritima
4.3.2.2
-
Pyrobaculum aerophilum

Protein Variants

EC Number Protein Variants Comment Organism
4.3.2.2 D422Y mutant without enzyme activity Homo sapiens
4.3.2.2 D430N mutant without enzyme activity Homo sapiens
4.3.2.2 L423V mutant without enzyme activity Homo sapiens
4.3.2.2 P110A/D422Y heat sensitive mutant Homo sapiens
4.3.2.2 R141W thermostable mutant with decreased activity Homo sapiens
4.3.2.2 R303C thermostable mutant with decreased activity Homo sapiens
4.3.2.2 R426H mutant without enzyme activity Homo sapiens
4.3.2.2 S395R thermostable mutant with decreased activity Homo sapiens
4.3.2.2 S438P heat sensitive mutant without enzyme activity Homo sapiens

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.3.2.2 additional information dithiothreitol increases inhibition of trans-4-hydroxy-2-nonenal; hydroxylamine reverses inhibition of trans-4-hydroxy-2-nonenal Bacillus subtilis
4.3.2.2 additional information dithiothreitol increases inhibition of trans-4-hydroxy-2-nonenal; hydroxylamine reverses inhibition of trans-4-hydroxy-2-nonenal Homo sapiens
4.3.2.2 additional information dithiothreitol increases inhibition of trans-4-hydroxy-2-nonenal; hydroxylamine reverses inhibition of trans-4-hydroxy-2-nonenal Pyrobaculum aerophilum
4.3.2.2 additional information dithiothreitol increases inhibition of trans-4-hydroxy-2-nonenal; hydroxylamine reverses inhibition of trans-4-hydroxy-2-nonenal Thermotoga maritima
4.3.2.2 nonenal
-
Bacillus subtilis
4.3.2.2 nonenal
-
Homo sapiens
4.3.2.2 nonenal
-
Pyrobaculum aerophilum
4.3.2.2 nonenal
-
Thermotoga maritima
4.3.2.2 trans-4-hydroxy-2-nonenal 10-15 µM, inhibitor reacts both with the free enzyme and the enzyme substrate complex Bacillus subtilis
4.3.2.2 trans-4-hydroxy-2-nonenal 10-15 µM, inhibitor reacts both with the free enzyme and the enzyme substrate complex Homo sapiens
4.3.2.2 trans-4-hydroxy-2-nonenal 10-15 µM, inhibitor reacts both with the free enzyme and the enzyme substrate complex Pyrobaculum aerophilum
4.3.2.2 trans-4-hydroxy-2-nonenal 10-15 µM, inhibitor reacts both with the free enzyme and the enzyme substrate complex Thermotoga maritima

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.3.2.2 5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide Bacillus subtilis
-
5-aminoimidazole-4-carboxamide ribonucleotide + fumarate
-
?
4.3.2.2 5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide Homo sapiens
-
5-aminoimidazole-4-carboxamide ribonucleotide + fumarate
-
?
4.3.2.2 5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide Thermotoga maritima
-
5-aminoimidazole-4-carboxamide ribonucleotide + fumarate
-
?
4.3.2.2 5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide Pyrobaculum aerophilum
-
5-aminoimidazole-4-carboxamide ribonucleotide + fumarate
-
?
4.3.2.2 adenylosuccinate Bacillus subtilis
-
AMP + fumarate
-
?
4.3.2.2 adenylosuccinate Homo sapiens
-
AMP + fumarate
-
?
4.3.2.2 adenylosuccinate Thermotoga maritima
-
AMP + fumarate
-
?
4.3.2.2 adenylosuccinate Pyrobaculum aerophilum
-
AMP + fumarate
-
?

Organism

EC Number Organism UniProt Comment Textmining
4.3.2.2 Bacillus subtilis
-
-
-
4.3.2.2 Homo sapiens
-
-
-
4.3.2.2 Pyrobaculum aerophilum
-
-
-
4.3.2.2 Thermotoga maritima
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.3.2.2 5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide
-
Bacillus subtilis 5-aminoimidazole-4-carboxamide ribonucleotide + fumarate
-
?
4.3.2.2 5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide
-
Homo sapiens 5-aminoimidazole-4-carboxamide ribonucleotide + fumarate
-
?
4.3.2.2 5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide
-
Thermotoga maritima 5-aminoimidazole-4-carboxamide ribonucleotide + fumarate
-
?
4.3.2.2 5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide
-
Pyrobaculum aerophilum 5-aminoimidazole-4-carboxamide ribonucleotide + fumarate
-
?
4.3.2.2 adenylosuccinate
-
Bacillus subtilis AMP + fumarate
-
?
4.3.2.2 adenylosuccinate
-
Homo sapiens AMP + fumarate
-
?
4.3.2.2 adenylosuccinate
-
Thermotoga maritima AMP + fumarate
-
?
4.3.2.2 adenylosuccinate
-
Pyrobaculum aerophilum AMP + fumarate
-
?

Subunits

EC Number Subunits Comment Organism
4.3.2.2 homotetramer
-
Bacillus subtilis
4.3.2.2 homotetramer
-
Homo sapiens
4.3.2.2 homotetramer
-
Thermotoga maritima
4.3.2.2 homotetramer
-
Pyrobaculum aerophilum

Synonyms

EC Number Synonyms Comment Organism
4.3.2.2 ADSL
-
Bacillus subtilis
4.3.2.2 ADSL
-
Thermotoga maritima
4.3.2.2 ADSL
-
Pyrobaculum aerophilum