The DOI matches its Crossref record; 12 of the 12 references it cites were found in a registry or an index.
Pyruvoyl-dependent histidine decarboxylases. Mechanism of cleavage of the proenzyme from Lactobacillus buchneri.
Open accessAbstract
When Lactobacillus buchneri was grown in the presence of [hydroxyl-18O]serine and pyridoxamine, no 18O was found in its histidine decarboxylase (HisDCase). However, when pyridoxamine was omitted from the growth medium, the labeled serine was incorporated into the HisDCase without dilution. Internal serine residues of the enzyme contained 18O only in their hydroxyl group, while the COOH-terminal serine of the beta chain of HisDCase contained equal amounts of 18O in both its hydroxyl and carboxyl group. This enzyme, like the HisDCase from Lactobacillus 30a (Recsei, P. A., Huynh, Q. K., and Snell, E. E. (1983) Proc. Natl. Acad. Sci. U.S.A. 80, 973-977), therefore, arises by nonhydrolytic serinolysis of its proenzyme. This result, together with comparative sequence data (Huynh, Q. K., and Snell, E. E. (1985) J. Biol. Chem. 260, 2798-2803), makes it highly probable that all of the pyruvoyl-dependent HisDCases arise by a similar mechanism from inactive proenzymes.
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“some LAB, besides TPP-dependent-acid decarboxylases, also bear PLP-or pyruvoil-dependent amino acid decarboxylases that can generate undesired amines, depending on the precursor amino acid present at this fermentation stage (Recsei and Snell, 1985).”
From Bioactive Molecules Released in Food by Lactic Acid Bacteria: Encrypted Peptides and Biogenic Amines (2016) · cites this paper as Recsei and Snell, 1985
Citations
Cites
Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
LAEMMLI, U. K. (1970) · Nature · doi:10.1038/227680a0 · Cited by 249,961
A Simple Chromatographic Method for Preparation of Gamma Globulin.
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Rescei, P., & Snell, E. E. (1984) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.53.070184.002041 · Cited by 115
Self-citationChang, G. W., & Snell, E. E. (1968) · Biochemistry · doi:10.1021/bi00846a001 · Cited by 86
Self-citationSOME CHEMICAL FACTORS WHICH INFLUENCE THE AMINO ACID REQUIREMENTS OF THE LACTIC ACID BACTERIA
Lyman, C. M., Moseley, O., Wood, S., et al. (1947) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)35154-2 · Cited by 78
GROWTH PROMOTION BY KETO AND HYDROXY ACIDS AND ITS RELATION TO VITAMIN B6
Holden, J. T., Wildman, R. B., & Snell, E. E. (1951) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)55961-5 · Cited by 74
Self-citationRecsei, P. A., Huynh, Q. K., & Snell, E. E. (1983) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.80.4.973 · Cited by 66
Self-citationPurification and properties of histidine decarboxylase from Lactobacillus 30a.
Rosenthaler, J., Guirard, B. M., Chang, G. W., et al. (1965) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.54.1.152 · Cited by 61
Huynh, Q. K., & Snell, E. E. (1985) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)89433-9 · Cited by 32
Self-citationRecsei, P. A., & Snell, E. E. (1982) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)34556-3 · Cited by 31
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Bioactive Molecules Released in Food by Lactic Acid Bacteria: Encrypted Peptides and Biogenic Amines
Pessione, E., & Cirrincione, S. (2016) · Frontiers in Microbiology · doi:10.3389/fmicb.2016.00876 · Cited by 333
A proteomic approach to studying biogenic amine producing lactic acid bacteria.
Pessione, E., Mazzoli, R., Giuffrida, M. G., Lamberti, C., Garcia‐Moruno, E., Barello, C., Conti, A., & Giunta, C. (2005) · PROTEOMICS · doi:10.1002/pmic.200401116 · Cited by 103
Metadata
- Authors
- Recsei, P. A., & Snell, E. E.
- Affiliations
- Rockefeller University (US)
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1985-03
- Volume
- 260
- Issue
- 5
- Pages
- 2804-2806
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1509333448
- Cited by
- 26
- References
- 12
- Citations by year
- 2025: 1 · 2024: 1 · 2016: 2 · 2015: 1 · 2014: 1 · 2013: 1
- FWCI
- 1.27
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (5r01am019898-10)
- National Institute of Allergy and Infectious Diseases (AI 13940)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Amino Acid Enzymes and Metabolism
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Molecular Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
- Keywords
- histidine decarboxylase, Lactobacillus buchneri, pyridoxamine, 18O labeling, serine incorporation, enzyme activation mechanism, pyruvate decarboxylase
- MeSH terms
- Amino Acid Sequence, Carboxy-Lyases, Enzyme Precursors, Histidine Decarboxylase, Lactobacillus, Pyridoxamine, Pyruvates, Serine, Mass Spectrometry, Pyruvic Acid
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