Cited by 51Microbial metabolism and enzyme functionEnzyme Structure and FunctionAmino Acid Enzymes and Metabolism

Purification and Characterization of Protein PB of Betaine Reductase and its Relationship to the Corresponding Proteins Glycine Reductase and Sarcosine Reductase from Eubacterium Acidaminophilum

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Meyer, Manfred, Granderath, Katrin, Andreesen, Jan R.·1995·European Journal of Biochemistry

Abstract

Simple complementation assay systems were developed for the substrate‐specific proteins P B of glycine reductase, sarcosine reductase, and betaine reductase, in which acetyl phosphate was detected as the product in all three cases. The betaine‐specific subunits of protein B (P B betaine) responsible for betaine reductase activity were purified to homogeneity from cells of Eubacterium acidaminophilum. The molecular masses of the two different subunits were 45 kDa and 48 kDa according to SDS/PAGE. The molecular mass of the native protein was about 200 kDa, indicating an α 2 β 2 structure. The glycine‐specific protein B (P B glycime) was partially purified and subunits of 47 kDa and 27 kDa were N‐terminally sequenced. The latter subunits cross‐reacted with antibodies raised against P B betaine and showed high sequence similarity to the 45‐kDa and 48‐kDa subunits of P B betaine, respectively. (2‐14 C]Glycine could be covalently coupled to the 47‐kDa subunit by treatment with borohydride. By the same procedure, [2‐14 C]sarcosine labeled a protein of the same size. Like the sarcosine reductase activity, this protein was not present in glycine‐grown cells, indicating its specific involvement in sarcosine metabolism. The labile viologen‐dependent formate dehydrogenase purified with the respective P B proteins and could be tentatively assigned to a 95‐kDa protein.

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  1. Granderath, K. (1988) Physiologische und enzymatische Unter- suchungen zum Abbau von Aminosiuren und organischen Siuren durch Eubacterium aci(kEnzinoplzilum, Diploma thesis, University of Gijttingen.
  2. Friedebold, J. (1994) Das Formiat-oxidierende Enzymsystem in Alcnligenes eutrojihus: Biochemische Charakterisierung der loslichen Formiat-Dehydrogenase, Ph.D. Thesis, University of Gottingen.
  3. Bliidorn, B. (1993) Isolierung eines 63 kDa-Proteins und vergleichende Charakterisierungen mit der Acetat-Kinase aus Eubacleriuin cici~r/nikr)phiIuln. Diploma thesis. University of Gottingen.
  4. Rieth, M. (1987) Untersuchungen m r selenabhangigen Glycin-Re- duktase aus Euhacterium acidaminophilum, Ph.D. Thesis, Univer- sity of Gottingen.

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Authors
Meyer, M., Granderath, K., & Andreesen, J. R.
Affiliations
  • University of Göttingen (DE)
  • Martin Luther University Halle-Wittenberg (DE)
Corresponding author
Andreesen, Jan R.
Venue
European Journal of Biochemistry
Publisher
Wiley
Published
1995-11
Volume
234
Issue
1
Pages
184-191
ISSN
  • 0014-2956 (ISSN-L)
  • 1432-1033
OpenAlex
W2143418808
Cited by
51
References
30
Citations by year
2026: 1 · 2025: 1 · 2024: 2 · 2023: 3 · 2021: 3 · 2020: 3 · 2019: 2 · 2018: 2 · 2017: 3 · 2016: 1 · 2015: 2 · 2014: 1 · 2012: 2
FWCI
0.62
Type
journal article
Language
en
Open access
Locations
  • European Journal of Biochemistry (publishedVersion)
  • PubMed (publishedVersion)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Microbial metabolism and enzyme function
  • Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Amino Acid Enzymes and Metabolism
Keywords
glycine reductase, protein B, protein purification, complementation assay, acetyl phosphate, glycine metabolism, protein subunit structure, N-terminal sequence
MeSH terms
Amino Acid Oxidoreductases, Amino Acid Sequence, Betaine, Electrophoresis, Polyacrylamide Gel, Eubacterium, Formate Dehydrogenases, Glycine, Molecular Sequence Data, Multienzyme Complexes, Sarcosine, Substrate Specificity

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