Crystal Structure of 1-Aminocyclopropane-1-carboxylate Deaminase from Hansenula saturnus

Yao, Ming; Ose, Toyoyuki; Sugimoto, Hiroshi; Horiuchi, Atsushi; Nakagawa, Atsushi; Wakatsuki, Soichi; Yokoi, Daisuke; Murakami, Tetuhide H.; Honma, M.; Tanaka, Isao

doi:10.1074/jbc.m004681200

Cited by 59 publications

(86 citation statements)

References 40 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…AtOASS, the bacterial OASS, and other enzymes requiring PLP as a cofactor share a common topology in the PLP-and substrate-binding domains (24,(32)(33)(34)(35)(36)(37). The overall ␣/␤-domain structure maintains the PLP binding site with sequence variations in the active site diversifying substrate recognition and reaction chemistry.…”

Section: Discussionmentioning

confidence: 99%

“…A search of the Protein Data Bank using DALI (31) showed that AtOASS shares a similar three-dimensional fold with E. coli threonine deaminase (32), S. typhimurium tryptophan synthase ␤-subunit (33), Sacchromyces cerevisiae threonine synthase (34), Arabidopsis threonine synthase (35), Rattus norvegicus serine dehydratase (36), and Hansenula saturnus 1-aminocyclopropane-1-carboxylate deaminase (37). AtOASS is related by 14 -21% amino acid sequence identity to these proteins with r.m.s.…”

Section: Three-dimensional Structurementioning

confidence: 99%

See 1 more Smart Citation

Molecular Basis of Cysteine Biosynthesis in Plants

Bonner

Cahoon

Knapke

et al. 2005

Journal of Biological Chemistry

171

View full text Add to dashboard Cite

Section: Discussionmentioning

confidence: 99%

Section: Three-dimensional Structurementioning

confidence: 99%

Molecular Basis of Cysteine Biosynthesis in Plants

Bonner

Cahoon

Knapke

et al. 2005

Journal of Biological Chemistry

171

View full text Add to dashboard Cite

“…ACP (26% identity, 40% similarity), Penicillium citrinum (26% identity, 39% similarity), and Hansenula saturnus (22% identity, 36% similarity) (26 -29). The similarity between NocJ and the ACC deaminases is not particularly strong, but careful analysis of the alignments with these proteins, however, revealed the greatest similarity was observed in the immediate vicinity of the lysine residue responsible for binding the PLP cofactor (30,31). Examination of the region surrounding the PLP-binding lysine revealed NocJ also contains a lysine at this position, corresponding to Lys 51 of the H. saturnus enzyme.…”

Section: Analysis Of Nocj-mentioning

confidence: 99%

Mutational Analysis and Characterization of Nocardicin C-9′ Epimerase

Kelly

Townsend

2004

Journal of Biological Chemistry

View full text Add to dashboard Cite

The biosynthetic gene cluster for the nocardicin A producer Nocardia uniformis subsp. tsuyamanensis ATCC 21806 was recently identified. Nocardicin A is the most potent of a series of monocyclic ␤-lactam antibiotics produced by this organism. Its activity has been attributed to a syn-configured oxime moiety and a D-homoseryl side chain attached through an unusual ether linkage to the core nocardicin framework. Notably present in the nocardicin biosynthetic gene cluster is nocJ, encoding a protein with sequence similarity to the pyridoxal 5 -phosphate (PLP)-dependent 1-aminocyclopropane-1-carboxylic acid deaminases. Insertional mutagenesis of nocJ abolished nocardicin A production, while the L-homoseryl isomer, isonocardicin A, was still observed. Expression of the disrupted nocJ gene in trans was sufficient to restore production of nocardicin A in the disruption mutant. Heterologous expression, purification, and in vitro characterization of NocJ by UV spectroscopy, cofactor reduction, chiral HPLC analysis of the products and their exchange behavior in deuterium oxide led to confirmation of its role as the PLP-dependent nocardicin C-9 epimerase responsible for interconversion of the nocardicin homoseryl side chain in both nocardicin A with isonocardicin A, and nocardicin C with isonocardicin C. NocJ is the first member of a new class of ␤-lactam aminoacyl side chain epimerases, the first two classes being the evolutionarily distinct prokaryotic PLP-dependent isopenicillin N epimerase and the fungal isopenicillin N epimerase two protein system.

show abstract

“…By analogy to the other enzymes, those extensions could be involved in regulation too. Very recently, Yao et al (2000) published the structure of aminocyclopropane carboxylate deaminase, which has a similar fold to domains 2 and 3 of TS and is not allosteric.…”

Section: Structure Comparison With Three Plp Enzymes Of the Second Fomentioning

confidence: 99%

Crystal structure of threonine synthase from Arabidopsis thaliana

Thomazeau

2001

Protein Science

View full text Add to dashboard Cite

Threonine synthase (TS) is a PLP-dependent enzyme that catalyzes the last reaction in the synthesis of threonine from aspartate. In plants, the methionine pathway shares the same substrate, O-phospho-Lhomoserine (OPH), and TS is activated by S-adenosyl-methionine (SAM), a downstream product of methionine synthesis. This positive allosteric effect triggered by the product of another pathway is specific to plants. The crystal structure of Arabidopsis thaliana apo threonine synthase was solved at 2.25 Å resolution from triclinic crystals using MAD data from the selenomethionated protein. The structure reveals a fourdomain dimer with a two-stranded ␤-sheet arm protruding from one monomer onto the other. This domain swap could form a lever through which the allosteric effect is transmitted. The N-terminal domain (domain 1) has a unique fold and is partially disordered, whereas the structural core (domains 2 and 3) shares the functional domain of PLP enzymes of the same family. It also has similarities with SAM-dependent methyltransferases. Structure comparisons allowed us to propose potential sites for pyridoxal-phosphate and SAM binding on TS; they are close to regions that are disordered in the absence of these molecules.Keywords: Allostery; MAD; pyridoxal phosphate; S-adenosyl-methionine; threonine synthesis Aspartate is a precursor for the synthesis of several other amino acids, including lysine, threonine, isoleucine, and methionine. Threonine synthase (TS) (EC 4.2.99.2) is the last enzyme of the threonine synthesis pathway (Fig. 1A). It is a PLP-dependent enzyme and a 110-kD homodimer in solution. It catalyzes the conversion of O-phospho-L-homoserine (OPH) into threonine and inorganic phosphate (Fig. 1B). The bacterial reaction was studied by following the absorbence of PLP and was shown to present at least seven steps (Laber et al. 1994).In plants, OPH is a branch point intermediate between the methionine/S-adenosyl-methionine (SAM) and threonine/ isoleucine pathways (Giovanelli et al. 1984). Thus TS competes for OPH with cystathionine-␥-synthase (CGS), the first committed enzyme in the methionine pathway (Fig. 1A). Flux regulation between the threonine and methionine pathways does not result from end-product inhibition but, rather, via a strong stimulation of TS by SAM (Giovanelli et al. 1984). Indeed, previous results showed that the allosteric binding of SAM leads to an eightfold increase in the rate of catalysis and to a 25-fold decrease in the K M value for OPH (Curien et al. 1998). Saturation isotherms of TS by SAM disclosed positive cooperativity and indicated that at least two SAM molecules can bind on each dimeric enzyme (Curien et al. 1998). From these results, it was concluded that the dramatic modification in kinetic properties of plant TS originates from an allosteric and cooperative transition that is induced by SAM. Furthermore, this transition occurs at a

show abstract

Crystal Structure of 1-Aminocyclopropane-1-carboxylate Deaminase from Hansenula saturnus

Cited by 59 publications

References 40 publications

Molecular Basis of Cysteine Biosynthesis in Plants

Molecular Basis of Cysteine Biosynthesis in Plants

Mutational Analysis and Characterization of Nocardicin C-9′ Epimerase

Crystal structure of threonine synthase from Arabidopsis thaliana

Contact Info

Product

Resources

About