N
            <sup>5</sup>
            ‐(1‐Carboxyethyl) Ornithine and Related (
            <i>n</i>
            ‐Carboxyalkyl)‐Amino Acids: Structure, Biosynthesis, and Function

Thompson, John F.; Miller, Stephen

doi:10.1002/9780470123102.ch7

Cited by 4 publications

(2 citation statements)

References 274 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Amino acid analysis has established that enzymes catalyzing product formation with (D,L) stereochemistry and those catalyzing product formation with (L,L) stereochemistry belong to two distinct protein subfamilies. 15 Furthermore, among one subfamily, sequence homology is around 20%-30%, while no significant homology exists between the two subfamilies.…”

Section: Introductionmentioning

confidence: 99%

A Structural Basis for Substrate Selectivity and Stereoselectivity in Octopine Dehydrogenase from Pecten maximus

Smits

Mueller

Schmitt

et al. 2008

Journal of Molecular Biology

View full text Add to dashboard Cite

Section: Introductionmentioning

confidence: 99%

A Structural Basis for Substrate Selectivity and Stereoselectivity in Octopine Dehydrogenase from Pecten maximus

Smits

Mueller

Schmitt

et al. 2008

Journal of Molecular Biology

View full text Add to dashboard Cite

“…This extensive hydrogen bond network presumably facilitates the orientation of pyruvic acid within the active site, thereby imposing a selective restraint upon the molecular size of ␣-keto acids that can serve as substrates in the condensation reaction ( Table 1). The catalytic functions of CEOS, and the biochemical role(s) of the N -(carboxyalkyl) products are currently unknown (15,18). Indeed, it is possible that neither ornithine nor lysine are the physiological in vivo targets of the reductive condensation reaction.…”

Section: Vol 192 2010 Notesmentioning

confidence: 99%

The Gene CBO0515 from Clostridium botulinum Strain Hall A Encodes the Rare Enzyme N ⁵ -(Carboxyethyl) Ornithine Synthase, EC 1.5.1.24

et al. 2010

Self Cite

View full text Add to dashboard Cite

Sequencing of the genome of Clostridium botulinum strain Hall A revealed a gene (CBO0515), whose putative amino acid sequence was suggestive of the rare enzyme N 5 -(1-carboxyethyl) ornithine synthase. To test this hypothesis, CBO0515 has been cloned, and the encoded polypeptide was purified and characterized. This unusual gene appears to be confined to proteolytic strains assigned to group 1 of C. botulinum.In the late 1980s, high concentrations of two unknown ninhydrin-reactive compounds were discovered in the amino acid pool of Lactococcus lactis, an organism used extensively for the manufacture of cheese in the dairy industry. The two compounds, subsequently identified as, were purified and characterized, and their stereochemical structures were established by chemical syntheses and nuclear magnetic resonance spectroscopy (11,14,17). These N-carboxyalkyl derivatives are formed enzymatically via a reductive condensation between pyruvic acid and the (side chain) amino groups of ornithine and lysine, respectively (Fig. 1).In L. lactis, the biosyntheses of N 5 -(CE) ornithine and N 6 -(CE) lysine are catalyzed by a unique tetrameric NADPHdependent enzyme, N 5

show abstract

The identification of three new biosynthetic intermediates and one further biosynthetic enzyme in the clavulanic acid pathway

Elson¹,

Baggaley²,

Davison³

et al. 1993

J. Chem. Soc., Chem. Commun.

View full text Add to dashboard Cite

Labelling experiments are described that identify three new compounds, N*-(2-carboxyethyl)arginine, 5-guanidino-(2-oxoazetidin-l-yl)pentanoic acid, and 3-hydroxy-5-guanidino-2-( 2-oxoazetidin-I -yl)pentanoic acid as biosynthetic precursors of proclavaminic acid and hence clavulanic acid in Streptom yces clavuligerus ATCC 27064 and a new amidino hydrolase, which hydrolyses 3-hydroxy-5-guanidino-2-(2-oxoazetidin-l -yl)pentanoic acid to proclavaminic acid has been characterised. As part of our goal to elucidate the biosynthesis of clavulanicAlso we reported4 on the production of two new arginine acid 11** we demonstrated3 that arginine 2 and not ornithine is derivatives 3 and 4 by the mutant S . clavuligerus dclH 65 which the amino acid that is processed into the biosynthetic pathway.is blocked in clavulanic acid biosynthesis. In addition, sequencing of the DNA of the clavulanic acid gene cluster identified an open reading frame, which showed homology to arginaseaS From these data we can postulate a number of possible biosynthetic sequences prior to prOClaVaminiC acid 5 which are shown in Scheme 1.

show abstract

N ⁵ ‐(1‐Carboxyethyl) Ornithine and Related ( n ‐Carboxyalkyl)‐Amino Acids: Structure, Biosynthesis, and Function

Cited by 4 publications

References 274 publications

A Structural Basis for Substrate Selectivity and Stereoselectivity in Octopine Dehydrogenase from Pecten maximus

A Structural Basis for Substrate Selectivity and Stereoselectivity in Octopine Dehydrogenase from Pecten maximus

The Gene CBO0515 from Clostridium botulinum Strain Hall A Encodes the Rare Enzyme N ⁵ -(Carboxyethyl) Ornithine Synthase, EC 1.5.1.24

The identification of three new biosynthetic intermediates and one further biosynthetic enzyme in the clavulanic acid pathway

Contact Info

Product

Resources

About

N 5 ‐(1‐Carboxyethyl) Ornithine and Related ( n ‐Carboxyalkyl)‐Amino Acids: Structure, Biosynthesis, and Function

Cited by 4 publications

References 274 publications

A Structural Basis for Substrate Selectivity and Stereoselectivity in Octopine Dehydrogenase from Pecten maximus

A Structural Basis for Substrate Selectivity and Stereoselectivity in Octopine Dehydrogenase from Pecten maximus

The Gene CBO0515 from Clostridium botulinum Strain Hall A Encodes the Rare Enzyme N 5 -(Carboxyethyl) Ornithine Synthase, EC 1.5.1.24

The identification of three new biosynthetic intermediates and one further biosynthetic enzyme in the clavulanic acid pathway

Contact Info

Product

Resources

About

N ⁵ ‐(1‐Carboxyethyl) Ornithine and Related ( n ‐Carboxyalkyl)‐Amino Acids: Structure, Biosynthesis, and Function

The Gene CBO0515 from Clostridium botulinum Strain Hall A Encodes the Rare Enzyme N ⁵ -(Carboxyethyl) Ornithine Synthase, EC 1.5.1.24