scholarly journals Betaine Stimulation of Vitamin B12 Biosynthesis in Pseudomonas denitrificans May Be Mediated by an Increase in Activity of  -Aminolaevulinic Acid Synthase

Microbiology ◽  
1984 ◽  
Vol 130 (4) ◽  
pp. 835-841
Author(s):  
J. P. Kusel ◽  
Y. H. Fa ◽  
A. L. Demain
Keyword(s):  
Vitamin B12 ◽  
Pseudomonas Denitrificans ◽  
Aminolaevulinic Acid ◽  
Stimulation Of

scholarly journals Biosynthesis of vitamin B12 in Pseudomonas denitrificans: the biosynthetic sequence from precorrin-6y to precorrin-8x is catalyzed by the cobL gene product.

1992 ◽  
Vol 174 (3) ◽  
pp. 1050-1052 ◽  
Author(s):  
F Blanche ◽  
A Famechon ◽  
D Thibaut ◽  
L Debussche ◽  
B Cameron ◽  
...  
Keyword(s):  
Vitamin B12 ◽  
Gene Product ◽  
Pseudomonas Denitrificans

Stimulation of vitamin B12 formation in aerobically-grownRhodopseudomonas gelatinosa under microaerobic condition

1986 ◽  
Vol 8 (7) ◽  
pp. 491-496 ◽  
Author(s):  
N. Noparatnaraporn ◽  
K. Sasaki ◽  
Y. Nishizawa ◽  
S. Nagai
Keyword(s):  
Vitamin B12 ◽  
Microaerobic Condition ◽  
Stimulation Of

scholarly journals Biosynthesis of vitamin B12: the preparative multi-enzyme synthesis of precorrin-3A and 20-methylsirohydrochlorin (a 2,7,20-trimethylisobacteriochlorin)

1996 ◽  
Vol 313 (1) ◽  
pp. 335-342 ◽  
Author(s):  
N. J. Patrick STAMFORD ◽  
Joël CROUZET ◽  
Béatrice CAMERON ◽  
Alex I. D. ALANINE ◽  
Andrew R. PITT ◽  
...  
Keyword(s):  
Vitamin B12 ◽  
Large Scale ◽  
Enzyme Preparation ◽  
Enzyme System ◽  
Enzyme Synthesis ◽  
High Yield ◽  
Pseudomonas Denitrificans ◽  
E Coli ◽  
Plasmid Construct ◽  
Porphobilinogen Synthase

The Bacillus subtilis genes hemB, hemC and hemD, encoding respectively the enzymes porphobilinogen synthase, hydroxymethylbilane synthase and uroporphyrinogen III synthase, have been expressed in Escherichia coli using a single plasmid construct. An enzyme preparation from this source converts 5-aminolaevulinic acid (ALA) preparatively and in high yield into uroporphyrinogen III. The Pseudomonas denitrificans genes cobA and cobI, encoding respectively the enzymes S-adenosyl-L-methionine:uroporphyrinogen III methyltransferase (SUMT) and S-adenosyl-L-methionine:precorrin-2 methyltransferase (SP2MT), were also expressed in E. coli. When SUMT was combined with the coupled-enzyme system that produces uroporphyrinogen III, precorrin-2 was synthesized from ALA, and when SP2MT was also added the product from the coupling of five enzymes was precorrin-3A. Both of these products are precursors of vitamin B12, and they can be used directly for biosynthetic experiments or isolated as their didehydro octamethyl esters in > 40% overall yield. The enzyme system which produces precorrin-3A is sufficiently stable to allow long incubations on a large scale, affording substantial quantities (15-20 mg) of product.

scholarly journals Betaine-Homocysteine Transmethylase in Pseudomonas denitrificans, a Vitamin B12 Overproducer

1973 ◽  
Vol 113 (1) ◽  
pp. 218-223 ◽  
Author(s):  
Raymond F. White ◽  
Louis Kaplan ◽  
Jerome Birnbaum
Keyword(s):  
Vitamin B12 ◽  
Pseudomonas Denitrificans

Revealing the promoting effect of betaine on vitamin B12 biosynthetic pathway of Pseudomonas denitrificans by using a proteomics analysis

2021 ◽  
Vol 22 ◽  
Author(s):  
Kun-tai Li ◽  
Yong Yang ◽  
Xin Cheng
Keyword(s):  
Vitamin B12 ◽  
Biosynthetic Pathway ◽  
Aminolevulinic Acid ◽  
Fermentation Medium ◽  
Promoting Effect ◽  
Pseudomonas Denitrificans ◽  
Methyl Group ◽  
Integral Effect ◽  
Comparative Metabolomics ◽  
Porphobilinogen Synthase

Background: Our previous comparative metabolomics research revealed that betaine (N,N,N-trimethylglycine, a typically essential methyl-group donor for vitamin B12 biosynthesis) had a powerful promoting effect on the generation of vitamin B12 precursors and intermediates in vitamin B12-producing Pseudomonas denitrificans. However, the integral effect of betaine on the vitamin B12 biosynthetic pathway is still unclear. Objective: Considering the vitamin B12 biosynthetic pathway of P. denitrificans as a whole, this work aimed to reveal the biological function of betaine on the vitamin B12 biosynthetic pathway in P. denitrificans, which would sharpen and expand the understanding of betaine as the methyl-group donor for vitamin B12 biosynthesis. Materials and Methods: By using a proteomics method based on the iTRAQ technique, the present study compared and analyzed the differential expression of proteins involved in vitamin B12 biosynthetic pathway under 10 g/L betaine addition to P. denitrificans fermentation medium. Results: The results showed that betaine could significantly up-regulate the expression of proteins related to the vitamin B12 biosynthetic pathway, which was mainly reflected in the following three aspects: 1) the δ-aminolevulinic acid (ALA) synthase and porphobilinogen synthase that were responsible for the formation of the committed precursors for tetrapyrrole-derived macrocycle in vitamin B12 molecule; 2) the C-methylation-related enzymes (such as precorrin-4 C(11)-methyltransferase, Precorrin-2 C(20)-methyltransferase, Precorrin-8X methylmutase, and Precorrin-6Y C5,15-methyltransferase) and methionine synthase that were crucial to the C-methylation reactions for vitamin B12 biosynthesis; 3) the late-stage key enzymes (Cobaltochelatase, and Cob(I)yrinic acid a,c-diamide adenosyltransferase) that were related to cobalt chelation of vitamin B12 molecule. Conclusions: The present study clearly demonstrated that betaine could significantly promote the expression of the integral enzymes involved in the vitamin B12 biosynthetic pathway of P. denitrificans, thus promoting vitamin B12 biosynthesis.

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