[18] Biosynthetic and biodegradative ornithine and arginine decarboxylases from Escherichia coli

Morris, David R.; Boeker, Elizabeth A.

doi:10.1016/s0076-6879(83)94020-x

Cited by 46 publications

(25 citation statements)

References 17 publications

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“…His-231, homologous to His-298 in ADC, appeared to play a role in hydrogen bonding of HDC to histidine or pyridoxal phosphate. Biodegradative ADC and LDC are similar in subunit size, molecular weight, and their pyridoxal phosphate-binding sequences (1,22). In these enzymes, pyridoxal phosphate binds to the e-amino group of the lysine residue within the conserved region, S-T-H-K-L-L (22).…”

Section: Discussionmentioning

confidence: 99%

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Nucleotide sequence and analysis of the speA gene encoding biosynthetic arginine decarboxylase in Escherichia coli

Moore

Boyle

1990

J Bacteriol

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The DNA sequence of a 3.23-kilobase fragment of the Escherichia coli chromosome encoding biosynthetic arginine decarboxylase (ADC) was determined. This sequence contained the speA open reading frame (ORF) as well as partial speB and metK ORFs. The ADC ORF is 1,974 nucleotides long; the deduced polypeptide contains 658 amino acids with a molecular size of 73,980 daltons. The molecular weight and predicted ADC amino acid composition are nearly identical to the amino acid analysis of purified ADC performed by Wu and Morris (J. Biol. Chem. 248:1687-1695, 1973). A translational speA-lacZ fusion, pRM65, including 1,389 base pairs (463 amino acids) of the 5' end of speA was constructed. Western blots (immunoblots) with beta-galactosidase antisera revealed two ADC::beta-galactosidase fusion proteins in E. coli bearing pRM65: 160,000 and 156,000 daltons representing precursor and mature hybrid proteins, respectively. The predicted amino acid sequence of ADC contains a region of six amino acid residues found in two bacterial diaminopimelic acid decarboxylases and three eucaryotic ornithine decarboxylases. This conserved sequence is located approximately eight amino acids from the putative pyridoxal phosphate-binding site of ADC and is predicted to be involved in substrate binding.

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Section: Discussionmentioning

confidence: 99%

“…Biodegradative ADC is induced in some strains of E. coli when they are grown in an acidic enriched medium containing arginine (9,22). Biodegradative amino acid decarboxylases appear to play a role in regulating pH by consuming protons and thus neutralizing the acidic products of carbohydrate fermentation (9).…”

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Nucleotide sequence and analysis of the speA gene encoding biosynthetic arginine decarboxylase in Escherichia coli

Moore

Boyle

1990

J Bacteriol

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“…The biosynthetic decarboxylases are constitutively expressed regardless of variations in pH and are involved in the synthesis of polyamines (57). The biodegradative decarboxylases, such as arginine and lysine decarboxylases, are strongly induced in rich medium at a low pH in the presence of excess substrate (4,5,21,39,44,52,57) and appear to play a role in pH homeostasis by consuming protons and neutralizing the acidic by-products produced during carbohydrate fermentation (22,49). Biodegradative arginine decarboxylase acts on arginine to produce agmatine and has been thoroughly characterized (5)(6)(7)(8)52).…”

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confidence: 99%

“…Relevant restriction sites are as follows: B, BamHI; D, DraI; E, EcoRI; GII, BglII; H, HindIII; P. PstI; RV, EcoRV; S, Salil. assayed for arginine decarboxylase activity by the method of Morris and Boeker (44).…”

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Nucleotide sequence of the adi gene, which encodes the biodegradative acid-induced arginine decarboxylase of Escherichia coli

Stim

Bennett

1993

J Bacteriol

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Arginine decarboxylase (encoded by adi) is induced under conditions of acidic pH, anaerobiosis, and rich medium. The DNA sequence of a 3-kb fragment of the Escherichia coli chromosome encoding biodegradative arginine decarboxylase was determined. This sequence encodes a protein of 755 amino acids with a molecular size of 84,420 daltons. The molecular weight and predicted Adi amino acid composition agree with those found in earlier work. The amino acid sequence of arginine decarboxylase showed homology to those of three other decarboxylases of E. cofi: (i) CadA, encoding lysine decarboxylase; (ii) SpeC, encoding biosynthetic ornithine decarboxylase; and (iii) SpeF, encoding biodegradative ornithine decarboxylase and the lysine decarboxylase of Hafnia alvei. Unlike SpeC and SpeF, Adi is not similar to the biosynthetic arginine decarboxylase, SpeA. adi is also dissimilar to cad4 and speF in that it does not appear to be part of an operon containing a metabolically related transport protein, indicating that it represents a new type of biodegradative decarboxylase regulation. Transcriptional fusions between fragments upstream of adi and lacZ, primer extension, and site-directed mutagenesis experiments defined the pH-regulated promoter. Deletion analysis of the upstream region and cloning of fragments to make adi::lacZ protein fusions implicated a region beyond an upstream SspI site in pH regulation. Induction of adi in the presence of sublethal concentrations of novobiocin or coumermycin Al, inhibitors of DNA gyrase, was dramatically decreased, indicating that DNA supercoiling is involved in adi expression. These results and those of promoter structure studies indicated that acid regulation of adi may involve a mechanism different from that of acid regulation of cad.

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“…The protein was isolated essentially as described by Morris & Boeker (1983) were grown using the hanging-drop method (McPherson, 1976). The protein droplet was made up of 10~tl of the protein solution [bADC at 25 mgm1-1 in 50mM potassium phosphate buffer (pH 7.0) containing 1 mM dithiothreitol, 5 mM magnesium sulfate and 40 mM PLP] mixed with 10~tl of the well solution (15% PEGS000 and 0.50 M lithium sulfate).…”

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Crystallization of biosynthetic arginine decarboxylase from Escherichia coli

et al. 1994

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Putrescine is the immediate precursor for the synthesis of polyamines and is normally generated by the action of ornithine decarboxylase. However, putrescine can also be produced by the conversion of arginine to agmatine by arginine decarboxylase (bADC) followed by the release of urea by agmatine ureohydrolase. Aminoacid sequence homology with the eukaryotic ornithine decarboxylases suggests that bADC may be a model for this group of decarboxylases. We report here the crystallization of arginine decarboxylase from E. coli. Crystals up to 1 mm in size are grown by vapor equilibration using Li2SO4 and polyethylene glycols as precipitants. The crystals exhibit diffraction maxima beyond 3/~ resolution and belong to space group P41(3)212 with a --192.4 and c --121.0 ]k. These unit-cell dimensions together with the estimated density of the crystals suggest the presence of one tetramer of bADC (71 kDa subunit-l) per asymmetric unit (Vm = 2.0,/k 3 Da-t).

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[18] Biosynthetic and biodegradative ornithine and arginine decarboxylases from Escherichia coli

Cited by 46 publications

References 17 publications

Nucleotide sequence and analysis of the speA gene encoding biosynthetic arginine decarboxylase in Escherichia coli

Nucleotide sequence and analysis of the speA gene encoding biosynthetic arginine decarboxylase in Escherichia coli

Nucleotide sequence of the adi gene, which encodes the biodegradative acid-induced arginine decarboxylase of Escherichia coli

Crystallization of biosynthetic arginine decarboxylase from Escherichia coli

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