Glycolaldehyde Is a Precursor of Pyridoxal Phosphate in Escherichia coli B

نویسندگان
چکیده

برای دانلود باید عضویت طلایی داشته باشید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Glycolaldehyde is a precursor of pyridoxal phosphate in Escherichia coli B.

Carbon-labeled glycolaldehyde prepared from [(14)C]serine was used to supply the nutritional requirement of a pyridoxineless auxotroph of Escherichia coli. Pyridoxal phosphate isolated from bacteria so grown was found to have incorporated the radioactive glycolaldehyde with little dilution. The radioactivity which was unincorporated into pyridoxal phosphate was recovered almost entirely in the ...

متن کامل

Pyridoxal 5′-Phosphate Is a Slow Tight Binding Inhibitor of E. coli Pyridoxal Kinase

Pyridoxal 5'-phosphate (PLP) is a cofactor for dozens of B(6) requiring enzymes. PLP reacts with apo-B(6) enzymes by forming an aldimine linkage with the ε-amino group of an active site lysine residue, thus yielding the catalytically active holo-B(6) enzyme. During protein turnover, the PLP is salvaged by first converting it to pyridoxal by a phosphatase and then back to PLP by pyridoxal kinase...

متن کامل

The Conversion of Pyridoxine Phosphate into Pyridoxal Phosphate in Escherichia Coli.

1. Evidence is presented for the presence of pyridoxine phosphate oxidase in aqueous extracts of Escherichia coli. Some comparison is made with pyridoxamine phosphate oxidase. 2. Isoniazid and iproniazid were found to combine with pyridoxal phosphate, but isoniazid did not combine with either pyridoxamine phosphate or pyridoxine phosphate. Both oxidase activities were somewhat inhibited by benz...

متن کامل

Pyridoxamine phosphate-oxidase and pyridoxal phosphate-phosphatase activities in Escherichia coli.

acetone), than found in earlier investigations. Mayer (1930) used a concentration of 66% for his determinations, but this is definitely inhibitory, though lese so for insoluble preparations than for soluble. The enzyme is remarkably stable before it becomes soluble and the activity of soluble preparations is retained well in the cold. The optimum temperature for enzyme action is much lower than...

متن کامل

Identification of amino acid residues modified by pyridoxal 5'-phosphate in Escherichia coli glutamine synthetase.

Chemical modification studies with pyridoxal 5'-phosphate have indicated that lysine(s) appear to be at or near the active site of Escherichia coli glutamine synthetase (Colanduoni, J., and Villafranca, J. J. (1985) J. Biol. Chem. 260, 15042-15050; Whitley, E. J., Jr., and Ginsburg, A. (1978) J. Biol. Chem. 253, 7017-7025). Enzyme samples were prepared that contained approximately 1, approximat...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

ژورنال

عنوان ژورنال: Journal of Bacteriology

سال: 1973

ISSN: 0021-9193,1098-5530

DOI: 10.1128/jb.116.1.341-345.1973