Crystallization and subunit structure of histidine decarboxylase from Lactobacillus 30a.
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چکیده
منابع مشابه
Crystallization and Subunit Structure of Histidine Decarboxylase
Histidine decarboxylase from Lactobacillus 30u has been crystallized in a variety of forms which together indicate a revised subunit structure for the native particle. Octahedral crystals of the wild type enzyme obtained at room temperature from ammonium sulfate solutions in microdiffusion cells belong to tetragonal space group 14122 with a = b = 222 A and c = 107.5 A. Trigonal and hexagonal pl...
متن کاملStructure and cooperativity of a T-state mutant of histidine decarboxylase from Lactobacillus 30a.
Histidine decarboxylase (HDC) from Lactobacillus 30a converts histidine to histamine, a process that enables the bacteria to maintain the optimum pH range for cell growth. HDC is regulated by pH; it is active at low pH and inactive at neutral to alkaline pH. The X-ray structure of HDC at pH 8 revealed that a helix was disordered, resulting in the disruption of the substrate-binding site. The HD...
متن کاملNutritional Requirements of Lactobacillus 30a for Growth and Histidine Decarboxylase Production.
Guirard, Beverly M. (University of California, Berkeley), and Esmond E. Snell. Nutritional requirements of Lactobacillus 30a for growth and histidine decarboxylase production. J. Bacteriol. 87:370-376. 1964.-The nutritional requirements of Lactobacillus 30a include each of the naturally occurring amino acids, several B vitamins, ascorbic acid, glucose, acetate, and oleate. The nutritional requi...
متن کاملpH-induced structural changes regulate histidine decarboxylase activity in Lactobacillus 30a.
Histidine decarboxylase (HDC) from Lactobacillus 30a produces histamine that is essential to counter waste acids, and to optimize cell growth. The HDC trimer is active at low pH and inactive at neutral to alkaline pH. We have solved the X-ray structure of HDC at pH 8 and revealed the novel mechanism of pH regulation. At high pH helix B is unwound, destroying the substrate binding pocket. At aci...
متن کاملHistidine decarboxylase of Lactobacillus 30a. Comparative sequences of the beta chain from wild type and mutant enzymes.
Manual and automated sequencing of peptides isolated from tryptic, chymotryptic, and Staphylococcus aureus V8 protease digests of the beta chain of histidine decarboxylase from Lactobacillus 30a have established the following sequence for the wild type protein: NH2-Ser-Gly-Leu-Asp-Ala-Lys-Leu-Asn-Lys-Leu-Gly-Val-Asp-Arg-Ile-Ala-Ile-Ser-Pro -Tyr-Lys-Gln-Trp-Thr-Arg-Gly-Tyr-Met-Glu-Pro-Gly-Asn-Il...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1981
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)70028-3