3.8.1.2: (S)-2-haloacid dehalogenase

This is an abbreviated version!
For detailed information about (S)-2-haloacid dehalogenase, go to the full flat file.

Reaction

Synonyms

2-HAD, 2-halo acid dehalogenase, 2-haloacid dehalogenase, 2-haloacid dehalogenase[ambiguous], 2-haloacid halidohydrolase[ambiguous], 2-haloalkanoate dehalogenase, 2-haloalkanoic acid dehalogenase, 2-haloalkanoid acid halidohydrolase, 2-halocarboxylic acid dehalogenase II, DEH99, dehalogenase IVa, DehL, DL-2-haloacid dehalogenase [ambiguous], HADIIBSW, HadL AJ1, L-2-DhlB, L-2-haloacid dehalogenase, L-2-MCPA dehalogenase, L-2_HAD, L-DEX, L-DEX YL, L-DEXs, L-HAD, L-HADST, L-haloacid dehalogenase, PH1421, Rhodobacteraceae family L-haloacid dehalogenase, S-2-haloacid dehalogenase, STK_25700

ECTree

     3 Hydrolases

         3.8 Acting on halide bonds

             3.8.1 In carbon-halide compounds

                3.8.1.2 (S)-2-haloacid dehalogenase

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Results	in table
10858	AA Sequence
23	Application
1	CAS Registry Number
21	Cloned(Commentary)
13	Crystallization (Commentary)
8	General Information
1	General Stability
29	Inhibitors
27	KM Value [mM]
3	Localization
7	Metals/Ions
46	Molecular Weight [Da]
90	Natural Substrates/ Products (Substrates)
28	Organic Solvent Stability
261	Organism
7	Pathway
55	PDB ID
20	pH Optimum
6	pH Range
6	pH Stability
6	pI Value
39	Protein Variants
23	Purification (Commentary)
17	Reaction
3	Reaction Type
99	Reference
4	Source Tissue
26	Specific Activity [micromol/min/mg]
4	Storage Stability
325	Substrates and Products (Substrate)
30	Subunits
68	Synonyms
1	Systematic Name
16	Temperature Optimum [°C]
9	Temperature Range [°C]
16	Temperature Stability [°C]
4	Turnover Number [1/s]

General Information

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General Information on EC 3.8.1.2 - (S)-2-haloacid dehalogenase

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GENERAL INFORMATION

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

evolution

6 entries

physiological function

Hymeniacidon perlevis

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DEH99 is a (S)-2-haloacid dehalogenase, which can degrade (S)-2-chloropropionic acid, (S)-2-bromopropionic acid, and iodoacetic acid

719748

additional information

Rhodobacteraceae bacterium UDC319

M9P6K0

folding of the DehRhb monomer and active site structure with catalytic residue Asp18, overall structure modeling. The halogen cradle in enzyme DehRhb is formed by the side chains of Phe47, Ile51, Phe66, Asn125 and Trp185

733826

evolution

Hymeniacidon perlevis

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the enzyme belongs to the Group II family

719748

evolution

Pseudomonas sp.

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the enzyme belongs to the HAD superfamily

719121

evolution

Pseudoalteromonas sp.

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2-HADs can be classified into two phylogenetically distinct groups according to their substrate specificity. Group II consists of only L-HADs, which selectively act on L-2-haloalkanoic acids to produce D-2-hydroxyacids. HADIIBSW is evolutionarily distinct from previously characterized L-HADs, sharing only 34% identity with L-HAD (DehRhb) from a Rhodobacteraceae family bacterium UDC319 as the closest relative

735151

evolution

Rhodobacteraceae bacterium UDC319

M9P6K0

the enzyme belongs to the HAD enzyme superfamily, which use an aspartate group as the nucleophile in their catalytic mechanism.. The HAD superfamily of enzymes also includes phosphate monoesterases, ATPases, phosphonoacetaldehyde hydrolases and phosphomutases

733826

evolution

Pseudomonas sp. 113

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the enzyme belongs to the HAD superfamily

-

evolution

Pseudoalteromonas sp. BSW20308

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2-HADs can be classified into two phylogenetically distinct groups according to their substrate specificity. Group II consists of only L-HADs, which selectively act on L-2-haloalkanoic acids to produce D-2-hydroxyacids. HADIIBSW is evolutionarily distinct from previously characterized L-HADs, sharing only 34% identity with L-HAD (DehRhb) from a Rhodobacteraceae family bacterium UDC319 as the closest relative

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