(Q27932653)

Journal of Biological Chemistry

GOA release 2020-03-11

author name string

Shinichi Taoka

series ordinal

1

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Ruma Banerjee

series ordinal

2

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language of work or name

English

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publication date

21 June 2002

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published in

1 reference

1 December 2016

277

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issue

25

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page(s)

22421-5

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cites work

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Folate, vitamin B12, and serum total homocysteine levels in confirmed Alzheimer disease.

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Cystathionine beta-synthase mutations in homocystinuria

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Evolutionary relationships among pyridoxal-5'-phosphate-dependent enzymes. Regio-specific alpha, beta and gamma families

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Modeling of the spatial structure of eukaryotic ornithine decarboxylases

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Structure of human cystathionine beta-synthase: a unique pyridoxal 5'-phosphate-dependent heme protein

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Three-dimensional structure of O-acetylserine sulfhydrylase from Salmonella typhimurium

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Structure and control of pyridoxal phosphate dependent allosteric threonine deaminase

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Mercuric chloride-induced spin or ligation state changes in ferric or ferrous human cystathionine beta-synthase inhibit enzyme activity

21 January 2018

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Characterization of NO binding to human cystathionine beta-synthase: possible implications of the effects of CO and NO binding to the human enzyme

21 January 2018

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Effects of heme ligand mutations including a pathogenic variant, H65R, on the properties of human cystathionine beta-synthase

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The reaction of yeast cystathionine beta-synthase is rate-limited by the conversion of aminoacrylate to cystathionine

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Tissue sulfhydryl groups

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Yeast cystathionine beta-synthase is a pyridoxal phosphate enzyme but, unlike the human enzyme, is not a heme protein

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Pyridoxal 5'-phosphate-dependent alpha,beta-elimination reactions: mechanism of O-acetylserine sulfhydrylase

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Pyridoxal phosphate binding sites are similar in human heme-dependent and yeast heme-independent cystathionine beta-synthases. Evidence from 31P NMR and pulsed EPR spectroscopy that heme and PLP cofactors are not proximal in the human enzyme

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