F
IPR002220

DapA-like

InterPro entry
Short nameDapA-like
Overlapping
homologous
superfamilies
 
family relationships

Description

Dihydrodipicolinate synthase (
4.2.1.52
) (DHDPS, DapA) catalyses, in higher plants, some fungi and bacteria (gene dapA), the first reaction specific to the biosynthesis of lysine and of diaminopimelate
[6]
. DHDPS is responsible for the condensation of aspartate semialdehyde and pyruvate by a ping-pong mechanism in which pyruvate first binds to the enzyme by forming a Schiff-base with a lysine residue
[5, 2]
.

Other proteins are structurally related to DHDPS and probably also act via a similar catalytic mechanism
[4]
:


 * Escherichia coli N-acetylneuraminate lyase (EC 4.1.3.3) (gene nanA), which catalyses the condensation of N-acetyl-D-mannosamine and pyruvate to form N-acetylneuraminate.
 * Trans-o-hydroxybenzylidenepyruvate hydratase-aldolase.
 * D-4-deoxy-5-oxoglucarate dehydratase.
 * Rhizobium meliloti protein mosA
[3]
, which is involved in the biosynthesis of the rhizopine 3-o-methyl-scyllo-inosamine.
 * Thermoproteus tenax 2-dehydro-3-deoxy-D-gluconate/2-dehydro-3-deoxy-phosphogluconate aldolase (KdgA)
[1]
.

References

1.Crystal structure and stereochemical studies of KD(P)G aldolase from Thermoproteus tenax. Pauluhn A, Ahmed H, Lorentzen E, Buchinger S, Schomburg D, Siebers B, Pohl E. Proteins 72, 35-43, (2008). View articlePMID: 18186475

2.New insights into the mechanism of dihydrodipicolinate synthase using isothermal titration calorimetry. Muscroft-Taylor AC, Soares da Costa TP, Gerrard JA. Biochimie 92, 254-62, (2010). View articlePMID: 20025926

3.The Rhizobium meliloti rhizopine mos locus is a mosaic structure facilitating its symbiotic regulation. Murphy PJ, Trenz SP, Grzemski W, De Bruijn FJ, Schell J. J. Bacteriol. 175, 5193-204, (1993). View articlePMID: 8349559

4.Structure and mechanism of a sub-family of enzymes related to N-acetylneuraminate lyase. Lawrence MC, Barbosa JA, Smith BJ, Hall NE, Pilling PA, Ooi HC, Marcuccio SM. J. Mol. Biol. 266, 381-99, (1997). View articlePMID: 9047371

5.Escherichia coli dihydrodipicolinate synthase. Identification of the active site and crystallization. Laber B, Gomis-Ruth FX, Romao MJ, Huber R. Biochem. J. 288 ( Pt 2), 691-5, (1992). View articlePMID: 1463470

6.Cloning, expression, purification and crystallization of dihydrodipicolinate synthase from Agrobacterium tumefaciens. Atkinson SC, Dogovski C, Dobson RC, Perugini MA. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 68, 1040-7, (2012). View articlePMID: 22949190

GO terms

biological process

  • None

molecular function

cellular component

  • None

Cross References

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