3.8.1.5: haloalkane dehalogenase

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

Reaction

Synonyms

1,3,4,6,-tetrachloro-1,4-cyclohexadiene halidohydrolase, 1-chlorohexane halidohydrolase, 1-haloalkane dehalogenase, DadB, DatA, DbeA, DbjA, DccA, DhaA, DhaA31, DhaB, DhaC, DhAf, DhlA, DhmA, DmaA, dmbA, DmbB, DmbC, dmlA, DmmA, DmrA, DmrB, DmsA, DmtA, DmxA, DpcA, DppA, DrbA, DsaA, DspA, EC 3.8.1.1, eHLD-B, eHLD-C, haloalkane dehalogenase, haloalkane dehalogenase LinB, HanR, HLD, HLD-I, LinB, LinBMI, LinBUT, metallo-haloalkane dehalogenase, protein XP_504164, Rv2579, Ylehd

ECTree

     3 Hydrolases

         3.8 Acting on halide bonds

             3.8.1 In carbon-halide compounds

                3.8.1.5 haloalkane dehalogenase

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Results	in table
4	Activating Compound
4440	AA Sequence
70	Application
1	CAS Registry Number
99	Cloned(Commentary)
51	Crystallization (Commentary)
8	Expression
136	General Information
4	General Stability
60	Inhibitors
62	kcat/KM [mM/s]
5	Ki Value [mM]
159	KM Value [mM]
4	Localization
2	Metals/Ions
28	Molecular Weight [Da]
64	Natural Substrates/ Products (Substrates)
21	Organic Solvent Stability
939	Organism
6	Pathway
148	PDB ID
57	pH Optimum
9	pH Range
4	pH Stability
2	pI Value
2	Posttranslational Modification
152	Protein Variants
57	Purification (Commentary)
51	Reaction
31	Reaction Type
288	Reference
2	Source Tissue
158	Specific Activity [micromol/min/mg]
1	Storage Stability
947	Substrates and Products (Substrate)
72	Subunits
323	Synonyms
1	Systematic Name
50	Temperature Optimum [°C]
4	Temperature Range [°C]
19	Temperature Stability [°C]
101	Turnover Number [1/s]

General Stability

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General Stability on EC 3.8.1.5 - haloalkane dehalogenase

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GENERAL STABILITY

ORGANISM

UNIPROT

LITERATURE

enzyme PEGylated with the thiosuccinimido butylamine linker shows the maximum resistance to high ionic strength (1 M NaCl)

Rhodococcus rhodochrous

P0A3G2

757271

glycerol stabilizes the enzyme

Yarrowia lipolytica

Q6C598

758396

immobilized enzyme exhibits a high stability in the extreme environmental conditions. The enzyme (DhaA) suffers from poor environmental stability and difficult recovery, which significantly increase the cost of DhaA. An effective enzyme immobilization strategy is developed to overcome the disadvantages of DhaA. DhaA is physically absorbed with amine-functionalized meso-cellular foam. The MCF-absorbed enzyme is intermolecularly crosslinked with 8-arm PEG N-hydroxysuccinimide ester and then PEGylated by maleimide-thiol chemistry

Rhodococcus rhodochrous

P0A3G2

756951

PEGylation with the thiosuccinimido butylamine linker significantly increases the stability of the enzyme

Rhodococcus rhodochrous

P0A3G2

757271