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PMID:4154089

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Citation

Guchhait, RB, Polakis, SE, Dimroth, P, Stoll, E, Moss, J and Lane, MD (1974) Acetyl coenzyme A carboxylase system of Escherichia coli. Purification and properties of the biotin carboxylase, carboxyltransferase, and carboxyl carrier protein components. J. Biol. Chem. 249:6633-45

Abstract

No abstract in PubMed

Links

PubMed

Keywords

Acetyl-CoA Carboxylase/isolation & purification; Acetyl-CoA Carboxylase/metabolism; Antimetabolites/pharmacology; Avidin; Bacterial Proteins/isolation & purification; Bacterial Proteins/metabolism; Bicarbonates; Binding Sites; Biotin; Carbon Radioisotopes; Cations, Divalent; Chromatography, Affinity; Chromatography, DEAE-Cellulose; Chromatography, Gel; Chromatography, Ion Exchange; Crystallization; Electrophoresis, Polyacrylamide Gel; Escherichia coli/enzymology; Kinetics; Ligases/metabolism; Molecular Weight; Multienzyme Complexes/isolation & purification; Multienzyme Complexes/metabolism; Protein Binding; Spectrophotometry, Ultraviolet; Transferases/isolation & purification; Transferases/metabolism; Ultracentrifugation

Significance

Annotations

Gene product Qualifier GO Term Evidence Code with/from Aspect Extension Notes Status

ECOLI:ACCC

GO:0016879: ligase activity, forming carbon-nitrogen bonds

ECO:0000314:

F

Table 1 and Experimental Procedure. Biotin carboxylase was purified and crystallized (Fig 1.). Biotin carboxylase activity was determined by 14C-bicarbonate fixation and spectrophotometric assay for 14C-labeled carboxybiotin. Biotin carboxylase activity involves forming a bond between an N on biotin and the C in HCO3-.

complete


See also

References

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