Autoxydation N<sup>2</sup>‐substituierter Methylhydrazine; Beeinflussung der Cu‐ &amp; Fe‐Katalyse durch Proteine, Desoxyribonucleinsäure (DNS) und EDTA

Aebi, H.; Dewald, Béatrice; Suter, Hedi

doi:10.1002/hlca.19650480403

Cited by 32 publications

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References 27 publications

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“…The effect of 5 mM phenylhydrazine on enzyme activity was followed only anaerobically under otherwise identical conditions, in order to prevent non-specific enzyme inactivation by hydrogen peroxide, which is formed from hydrazine derivatives in the presence of oxygen (Aebi et al, 1965). Table 1.…”

Section: Treatment With Nabb Hydroxylamine and Phenylhydrazinementioning

confidence: 99%

L‐Serine and L‐threonine dehydratase from Clostridium propionicum Two enzymes with different prosthetic groups

Hofmeister

Grabowski

Linder

1993

European Journal of Biochemistry

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L-Serine dehydratase from the Gram-positive bacterium Peptostreprococcus usuccharolyricus is novel in the group of enzymes deaminating 2-hydroxyamino acids in that it is an iron-sulfur protein and lacks pyridoxal phosphate [Grabowski, R. and Buckel, W. (1991) Eur. J. Biochem. 199, 89-941. It was proposed that this type of L-serine dehydratase is widespread among bacteria but has escaped intensive characterization due to its oxygen lability. Here, we present evidence that another Gram-positive bacterium, Clostridium pmpionicum, contains both an iron-sulfur-dependent L-serine dehydratase and a pyridoxal-phosphate-dependent L-threonine dehydratase. These findings support the notion that two independent mechanisms exist for the deamination of 2-hydroxyamino acids.L-Threonine dehydratase was purified 400-fold to apparent homogeneity and revealed as being a tetramer of identical subunits (m = 39 kDa). The purified enzyme exhibited a specific activity of 5 pkadmg protein and a K , for L-threonine of 7.7 mM. L-Serine ( K , = 380 mM) was also deaminated, the V/K, ratio, however, being 118-fold lower than the one for L-threonine. L-Threonine dehydratase was inactivated by borohydride, hydroxylamine and phenylhydrazine, all known inactivators of pyridoxal-phosphate-containing enzymes. Incubation with NaB3H, specifically labelled the enzyme. Activity of the phenylhydrazine-inactivated enzyme could be restored by pyridoxal phosphate.L-Serine dehydratase was also purified 400-fold, but its extreme instability did not permit purification to homogeneity. The enzyme was specific for L-serine ( K , = 5 mM) and was inhibited by L-cysteine (K, = 0.5 mM) and D-serine (K, = 8 mM). Activity was insensitive towards borohydride, hydroxylamine and phenylhydrazine but was rapidly lost upon exposure to air. Fez+ specifically reactivated the enzyme. L-Serine dehydratase was composed of two different subunits (a, m = 30kDa; p, m = 26kDa), their apparent molecular masses being similar to the ones of the two subunits of the iron-sulfur-dependent enzyme from Z? asuccharolyticus. Moreover, the N-terminal sequences of the small subunits from these two organisms were found to be 47% identical. In addition, 38% identity with the N-terminus of one of the two L-serine dehydratases of Escherichiu coli was detected.

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Section: Treatment With Nabb Hydroxylamine and Phenylhydrazinementioning

confidence: 99%

L‐Serine and L‐threonine dehydratase from Clostridium propionicum Two enzymes with different prosthetic groups

Hofmeister

Grabowski

Linder

1993

European Journal of Biochemistry

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Biological Formation and Reactions of Hydrazo, Azo and Azoxy Groups

Miyadera

The Chemistry of the Hydrazo, Azo and Azoxy Groups

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Biological formation and reactions of hydrazo, azo and azoxy groups

Miyadera

1975

PATAI'S Chemistry of Functional Groups

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Autoxydation N²‐substituierter Methylhydrazine; Beeinflussung der Cu‐ & Fe‐Katalyse durch Proteine, Desoxyribonucleinsäure (DNS) und EDTA

Abstract: 1. Autoxidation of natulan and other methylhydrazine derivatives has been investigated by WARBURG'S direct manometric method. These compounds are relatively stable in a heavy‐metal‐free environment at pH 7.0, but are rapidly oxidised if a suitable catalyst is added.

Cited by 32 publications

References 27 publications

L‐Serine and L‐threonine dehydratase from Clostridium propionicum Two enzymes with different prosthetic groups

L‐Serine and L‐threonine dehydratase from Clostridium propionicum Two enzymes with different prosthetic groups

Biological Formation and Reactions of Hydrazo, Azo and Azoxy Groups

Biological formation and reactions of hydrazo, azo and azoxy groups

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Autoxydation N2‐substituierter Methylhydrazine; Beeinflussung der Cu‐ & Fe‐Katalyse durch Proteine, Desoxyribonucleinsäure (DNS) und EDTA

Abstract: 1. Autoxidation of natulan and other methylhydrazine derivatives has been investigated by WARBURG'S direct manometric method. These compounds are relatively stable in a heavy‐metal‐free environment at pH 7.0, but are rapidly oxidised if a suitable catalyst is added.

Cited by 32 publications

References 27 publications

L‐Serine and L‐threonine dehydratase from Clostridium propionicum Two enzymes with different prosthetic groups

L‐Serine and L‐threonine dehydratase from Clostridium propionicum Two enzymes with different prosthetic groups

Biological Formation and Reactions of Hydrazo, Azo and Azoxy Groups

Biological formation and reactions of hydrazo, azo and azoxy groups

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Product

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About

Autoxydation N²‐substituierter Methylhydrazine; Beeinflussung der Cu‐ & Fe‐Katalyse durch Proteine, Desoxyribonucleinsäure (DNS) und EDTA