Serine Transhydroxymethylase

Schirch, LaVerne; Mason, Merle

doi:10.1016/s0021-9258(18)81254-6

Cited by 111 publications

(21 citation statements)

References 20 publications

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“…L-Cysteine reacts with pyridoxal 5'-phosphate to form a thiazolidine (Schirch & Mason, 1963), which has a UV absorption maximum at 335 nm, and can be used to prepare apoenzyme with many PLP-dependent enzymes. Cysteine is, however, unable to remove the pyridoxal S'-phosphate from AKB-ligase, but does form a 335 nm absorbing species, and the changes in UV absorption are cysteine dependent (Fubara et al, 1986).…”

Section: Resultsmentioning

confidence: 99%

2-Amino-3-ketobutyrate-CoA Ligase from Beef Liver Mitochondria: An NMR Spectroscopic Study of Low-Barrier Hydrogen Bonds of a Pyridoxal 5'-Phosphate-Dependent Enzyme

Tong¹,

Davis²

1995

Biochemistry

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A study of protons associated with low-barrier hydrogen bonds in 2-amino-3-ketobutyrate-CoA ligase (AKB-ligase, EC 2.3.1.29) by NMR is reported. Three resonances are observed in the range of delta H = 15-20 ppm when the NMR spectrum of AKB-ligase is recorded at 600 MHz. These low-barrier hydrogen bonds are associated respectively with a side chain proton, the PLP pyridinium ring nitrogen proton, and the PLP Schiff base proton at the active site of the ligase. The pyridinium proton has been assigned a chemical shift of 19.10 ppm and the Schiff base proton 14.90 ppm. The third low-barrier hydrogen bond associated proton resonating at 16.20 ppm is assigned to a proton of a side chain group. All three resonances disappear when pyridoxal phosphate is removed from the ligase. Consistent with NOE coupling, the side chain group proton should be close to the proton of the Schiff base nitrogen of the pyridoxal 5'-phosphate. The effects of temperature, pH, substrate, and NOE on the three resonances are also studied, in order to assign the protons. The three low-barrier hydrogen bonds described in this report may serve to anchor the cofactor in the active site of 2-amino-3-ketobutyrate-CoA ligase.

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Section: Resultsmentioning

confidence: 99%

2-Amino-3-ketobutyrate-CoA Ligase from Beef Liver Mitochondria: An NMR Spectroscopic Study of Low-Barrier Hydrogen Bonds of a Pyridoxal 5'-Phosphate-Dependent Enzyme

Tong¹,

Davis²

1995

Biochemistry

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“…Under these conditions Km for formate was 2.0 mM, Km for ATP was 2.3 X 10~4 m, and Km for l( ± )-tetrahydrofolate was 1.0 mM. There was an ab- This enzyme had a mol wt of 180,000 by the criteria of sucrose gradient centrifugation and Sephadex G-150 chromatography, a value which approximates the figure obtained by Fujioka (1969) for rabbit liver enzyme rather than the figure of 331,000 obtained by Schirch and Mason (1963). There was a broad pH optimum, maximal at pH 7.5, the activity profile again closely resembling that described by Nakano et al (1968) for the rat liver cytosol enzyme.…”

Section: Resultsmentioning

confidence: 57%

Mammalian folate metabolism. Regulation of folate interconversion enzymes

Rowe¹,

Lewis²

1973

Biochemistry

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Mechanisms of regulation of five of the enzymes central to the folate pathway in bovine liver have been examined. These enzymes, 10-formyltetrahydrofolate synthetase, serine transhydroxymethylase, dihydrofolate reductase, methylenetetrahydrofolate dehydrogenase, and methenyltetrahydrofolate cyclohydrolase were purified and their kinetic constants determined. None of the tested metabolites, associated with

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“…During the last several years a number of investigators have reported enzyme-substrate complexes of B6 enzymes absorbing near 495 µ (Jenkins, 1961a,b;Schirch and Mason, 1963;Marino and Snell, 1965). Schirch and Jenkins studied in some detail one of these complexes which is formed between D-alanine and serine transhydroxymethylase.…”

Section: Discussionmentioning

confidence: 99%

“…Several B8 enzymes have been found to form enzymesubstrate complexes which absorb near 495 µ (Jen- kins, 1961a,b; Schirch and Mason, 1963;Marino and Snell, 1965). Compounds formed between pyridoxal and amino acids in nonenzymatic systems have not been found to absorb at wavelengths in this region of the spectrum.…”

mentioning

confidence: 99%

Spectral Properties of Schiff Bases of Amino Acid Esters with Pyridoxal and Pyridoxal N-Methochloride in Ethanol^*

Schirch¹,

Slotter²

1966

Biochemistry

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Serine Transhydroxymethylase

Cited by 111 publications

References 20 publications

2-Amino-3-ketobutyrate-CoA Ligase from Beef Liver Mitochondria: An NMR Spectroscopic Study of Low-Barrier Hydrogen Bonds of a Pyridoxal 5'-Phosphate-Dependent Enzyme

2-Amino-3-ketobutyrate-CoA Ligase from Beef Liver Mitochondria: An NMR Spectroscopic Study of Low-Barrier Hydrogen Bonds of a Pyridoxal 5'-Phosphate-Dependent Enzyme

Mammalian folate metabolism. Regulation of folate interconversion enzymes

Spectral Properties of Schiff Bases of Amino Acid Esters with Pyridoxal and Pyridoxal N-Methochloride in Ethanol^*

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Serine Transhydroxymethylase

Cited by 111 publications

References 20 publications

2-Amino-3-ketobutyrate-CoA Ligase from Beef Liver Mitochondria: An NMR Spectroscopic Study of Low-Barrier Hydrogen Bonds of a Pyridoxal 5'-Phosphate-Dependent Enzyme

2-Amino-3-ketobutyrate-CoA Ligase from Beef Liver Mitochondria: An NMR Spectroscopic Study of Low-Barrier Hydrogen Bonds of a Pyridoxal 5'-Phosphate-Dependent Enzyme

Mammalian folate metabolism. Regulation of folate interconversion enzymes

Spectral Properties of Schiff Bases of Amino Acid Esters with Pyridoxal and Pyridoxal N-Methochloride in Ethanol*

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Product

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Spectral Properties of Schiff Bases of Amino Acid Esters with Pyridoxal and Pyridoxal N-Methochloride in Ethanol^*