F
IPR027278

1-aminocyclopropane-1-carboxylate deaminase/D-cysteine desulfhydrase

InterPro entry
Short nameACCD_DCysDesulf
Overlapping
homologous
superfamilies
 
family relationships

Description

This entry represents the 1-aminocyclopropane-1-carboxylate deaminase/D-cysteine desulfhydrase family. Proteins in this family include deaminase, D-cysteine desulfhydrase, phenylserine dehydratase and L-cysteate sulfo-lyase.

1-aminocyclopropane-1-carboxylate deaminase (
3.5.99.7
) catalyses a cyclopropane ring-opening reaction, the irreversible conversion of 1-aminocyclopropane-1-carboxylate (ACC) to ammonia and alpha-ketobutyrate
[1]
. Some plant growth-promoting rhizobacteria can produce 1-aminocyclopropane-1-carboxylate deaminase to enhance plant growth
[2, 3]
.

D-cysteine desulfhydrase (d-CDes) (
4.4.1.15
) catalyses the alpha, beta-elimination reaction of D-cysteine and of several D-cysteine derivatives. The Escherichia coli d-CDes catalyses D-cysteine into pyruvate, H2S, and NH3
[6, 5, 4]
. The physiological function of bacterial d-CDes is not clear.

References

1.Mechanistic studies of 1-aminocyclopropane-1-carboxylate deaminase: characterization of an unusual pyridoxal 5'-phosphate-dependent reaction. Thibodeaux CJ, Liu HW. Biochemistry 50, 1950-62, (2011). View articlePMID: 21244019

2.Plant growth-promoting rhizobacteria (PGPR): emergence in agriculture. Bhattacharyya PN, Jha DK. World J. Microbiol. Biotechnol. 28, 1327-50, (2012). PMID: 22805914

3.Metagenomic analysis of the 1-aminocyclopropane-1-carboxylate deaminase gene (acdS) operon of an uncultured bacterial endophyte colonizing Solanum tuberosum L. Nikolic B, Schwab H, Sessitsch A. Arch. Microbiol. 193, 665-76, (2011). View articlePMID: 21523387

4.Isolation and characterization of a D-cysteine desulfhydrase protein from Arabidopsis thaliana. Riemenschneider A, Wegele R, Schmidt A, Papenbrock J. FEBS J. 272, 1291-304, (2005). View articlePMID: 15720402

5.Physiological comparison of D-cysteine desulfhydrase of Escherichia coli with 3-chloro-D-alanine dehydrochlorinase of Pseudomonas putida CR 1-1. Nagasawa T, Ishii T, Yamada H. Arch. Microbiol. 149, 413-6, (1988). View articlePMID: 3132906

6.D-Cysteine desulfhydrase of Escherichia coli. Purification and characterization. Nagasawa T, Ishii T, Kumagai H, Yamada H. Eur. J. Biochem. 153, 541-51, (1985). View articlePMID: 3908101

Further reading

7. L-cysteate sulpho-lyase, a widespread pyridoxal 5'-phosphate-coupled desulphonative enzyme purified from Silicibacter pomeroyi DSS-3(T). Denger K, Smits TH, Cook AM. Biochem. J. 394, 657-64, (2006). View articlePMID: 16302849

Cross References

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