4.2.1.42: galactarate dehydratase

This is an abbreviated version!
For detailed information about galactarate dehydratase, go to the full flat file.

Word Map on EC 4.2.1.42

4.2.1.42

enolase

dehydration

racemase

mandelate

departure

agrobacterium

alpha-proton

aldolase

dyad

beta-strands

glycerate

d-galacturonate

analysis

seventh

epimerization

typhimurium

semialdehyde

Reaction

Synonyms

A9CG74, Dehydratase, galactarate, Galactarate dehydrase, galactarate dehydratase, galactarate dehydratase III, GalcD, GalrD, GalrD-III, L-talarate/galactarate dehydratase, m-galactarate dehydratase, STM3697

ECTree

4 Lyases

4.2 Carbon-oxygen lyases

4.2.1 Hydro-lyases

4.2.1.42 galactarate dehydratase

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Results	in table
3991	AA Sequence
4	Application
1	CAS Registry Number
6	Cloned(Commentary)
3	Crystallization (Commentary)
2	General Information
1	General Stability
6	Inhibitors
9	kcat/KM [mM/s]
2	Ki Value [mM]
10	KM Value [mM]
5	Metals/Ions
4	Natural Substrates/ Products (Substrates)
32	Organism
6	Pathway
6	PDB ID
3	pH Optimum
1	pH Range
11	Protein Variants
6	Purification (Commentary)
1	Reaction
1	Reaction Type
11	Reference
1	Specific Activity [micromol/min/mg]
20	Substrates and Products (Substrate)
18	Synonyms
1	Systematic Name
2	Temperature Optimum [°C]
9	Turnover Number [1/s]

Substrates Products

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Substrates Products on EC 4.2.1.42 - galactarate dehydratase

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D-Galactarate

5-Dehydro-4-deoxy-D-glucarate + H2O

4 entries

D-Galactarate

2 entries

D-galacturonate

3-deoxy-D-xylo-hexarate + 3-deoxy-D-lyxo-hexarate + H2O

2 entries

galactarate

(2R,3S)-2,3-dihydroxy-5-oxohexanedioate + H2O

4 entries

galactarate

5-dehydro-4-deoxy D-glucarate + H2O

Oceanobacillus iheyensis

702265

galactarate

5-dehydro-4-deoxy-D-glucarate + H2O

Salmonella enterica subsp. enterica serovar Typhimurium str. LT2

Q8ZL58

galactarate i.e. (2R,3S,4R,5S)-2,3,4,5-tetrahydroxyhexanedioate. The enzyme also catalyzes dehydration of L-talarate. The dehydration of L-talarate is accompanied by competing epimerization to galactarate. Little epimerization to L-talarate is observed in the dehydration of galactarate. On the basis of (1) structures of the wild type enzyme complexed with L-lyxarohydroxamate, an analogue of the enolate intermediate, and of the K197A mutant complexed with L-glucarate, a substrate for exchange of the R-proton, and (2) incorporation of solvent deuterium into galactarate in competition with dehydration, it is concluded that Lys197 functions as the galactarate-specific base and His328 functions as the L-talarate-specific base. The epimerization of L-talarate to galactarate that competes with dehydration can be rationalized by partitioning of the enolate intermediate between dehydration (departure of the 3-OH group catalyzed by the conjugate acid of His328) and epimerization (protonation on C2 by the conjugate acid of Lys197). Only galactarate and L-talarate are completely dehydrated by the enzyme. No other acid sugar results in detectable turnover

678325

L-talarate

5-dehydro-4-deoxy-D-glucarate + H2O

2 entries

meso-galactarate

2-dehydro-3-deoxy-D-glucarate + H2O

2 entries

meso-galactarate

5-dehydro-4-deoxy-D-glucarate + H2O

2 entries