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EC Number
BRENDA No.
Title
Journal
Volume
Pages
Year
Organism
PubMed ID
4.1.2.4
5162
The primary structure of Escherichia coli K12 2-deoxyribose 5-phosphate aldolase
Eur. J. Biochem.
125
561-566
1982
Escherichia coli
6749498
4.1.2.4
5163
Acrolein, an irreversible active-site-directed inhibitor of deoxyribose 5-phosphate aldolase?
Biochem. J.
153
495-497
1976
Salmonella enterica subsp. enterica serovar Typhimurium
776176
4.1.2.4
5164
Deoxyribose-5-phosphate aldolase from Salmonella typhimurium
Methods Enzymol.
42C
276-279
1975
Salmonella enterica subsp. enterica serovar Typhimurium
237187
4.1.2.4
5165
Deoxyribose-5-phosphate aldolase: subunit structure and composition of active site lysine region
Arch. Biochem. Biophys.
164
736-742
1974
Salmonella enterica subsp. enterica serovar Typhimurium
4618079
4.1.2.4
5166
Purification and properties of deoxyriboaldolase from human erythrocytes
Biochim. Biophys. Acta
212
478-487
1970
Homo sapiens
4989681
4.1.2.4
5167
2-Deoxyribose-5-phosphate aldolase of Salmonella typhimurium: purification and properties
Arch. Biochem. Biophys.
126
795-802
1968
Salmonella enterica subsp. enterica serovar Typhimurium
4879701
4.1.2.4
5168
Deoxyribose 5-phosphate aldolase. II. Purification and properties of the rat liver enzyme
J. Biol. Chem.
242
155-159
1967
Rattus norvegicus
6016328
4.1.2.4
5169
Deoxyribose 5-phosphate aldolase
Methods Enzymol.
9
549-554
1966
Rattus norvegicus
-
4.1.2.4
5170
Deoxyribose 5-phosphate aldolase. I. Lactobacillus plantarum
Methods Enzymol.
9
545-549
1966
Lactiplantibacillus plantarum
-
4.1.2.4
5171
The mechanism of action of aldolases. VII. Formation of a 2-methyl-2-deoxypentose catalyzed by deoxyribose 5-phosphate aldolase
J. Biol. Chem.
240
1517-1524
1965
Lactiplantibacillus plantarum
14285486
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