Purification, substrate specificity and binding, -decarboxylase activity, and other properties of Escherichia coli 2-keto-4-hydroxyglutarate aldolase
- PMID: 4560498
Purification, substrate specificity and binding, -decarboxylase activity, and other properties of Escherichia coli 2-keto-4-hydroxyglutarate aldolase
Similar articles
-
Variant properties of bovine liver 2-keto-4-hydroxyglutarate aldolase; its -decarboxylase activity, lack of substrate stereospecificity, and structural requirements for binding substrate analogs.Biochim Biophys Acta. 1971 Oct;250(1):238-50. doi: 10.1016/0005-2744(71)90139-2. Biochim Biophys Acta. 1971. PMID: 5168885 No abstract available.
-
2-Keto-4-hydroxyglutarate aldolase of bovine liver. Purification, criteria of purity, and general properties.J Biol Chem. 1969 Apr 10;244(7):1919-25. J Biol Chem. 1969. PMID: 5780845 No abstract available.
-
Formaldehyde binding by 2-keto-4-hydroxyglutarate aldolase. Formation and characterization of an inactive aldolase-formaldehyde-cyanide adduct.J Biol Chem. 1974 Aug 10;249(15):4891-6. J Biol Chem. 1974. PMID: 4858738 No abstract available.
-
A stereospecific 2-keto-4-hydroxyglutarate aldolase from Escherichia coli.Biochim Biophys Acta. 1969 Jul 8;185(1):255-7. doi: 10.1016/0005-2744(69)90303-9. Biochim Biophys Acta. 1969. PMID: 4894280 No abstract available.
-
N-acetylneuraminic acid aldolase of Clostridium perfringens: purification, properties and mechanism of action.Arch Biochem Biophys. 1972 Jul;151(1):234-42. doi: 10.1016/0003-9861(72)90493-6. Arch Biochem Biophys. 1972. PMID: 4339794 No abstract available.
Cited by
-
Cloning, nucleotide sequence, overexpression, and inactivation of the Escherichia coli 2-keto-4-hydroxyglutarate aldolase gene.J Bacteriol. 1992 Jan;174(1):102-7. doi: 10.1128/jb.174.1.102-107.1992. J Bacteriol. 1992. PMID: 1339418 Free PMC article.
-
Stereospecificity in meta-fission catabolic pathways.J Bacteriol. 1983 Jul;155(1):424-6. doi: 10.1128/jb.155.1.424-426.1983. J Bacteriol. 1983. PMID: 6345511 Free PMC article.
-
Covalent intermediate trapped in 2-keto-3-deoxy-6- phosphogluconate (KDPG) aldolase structure at 1.95-A resolution.Proc Natl Acad Sci U S A. 2001 Mar 27;98(7):3679-84. doi: 10.1073/pnas.071380898. Proc Natl Acad Sci U S A. 2001. PMID: 11274385 Free PMC article.
-
The synthetic xylulose-1 phosphate pathway increases production of glycolic acid from xylose-rich sugar mixtures.Biotechnol Biofuels. 2016 Sep 20;9:201. doi: 10.1186/s13068-016-0610-2. eCollection 2016. Biotechnol Biofuels. 2016. PMID: 27679669 Free PMC article.
-
Characterization of the 4-carboxy-4-hydroxy-2-oxoadipate aldolase gene and operon structure of the protocatechuate 4,5-cleavage pathway genes in Sphingomonas paucimobilis SYK-6.J Bacteriol. 2003 Jan;185(1):41-50. doi: 10.1128/JB.185.1.41-50.2003. J Bacteriol. 2003. PMID: 12486039 Free PMC article.
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources
Molecular Biology Databases