PMID- 9621448
OWN - NLM
STAT- MEDLINE
DCOM- 19980720
LR  - 20191102
IS  - 0141-0229 (Print)
IS  - 0141-0229 (Linking)
VI  - 22
IP  - 7
DP  - 1998 May 15
TI  - Biochemical characterization of a haloalcohol dehalogenase from Arthrobacter 
      erithii H10a.
PG  - 568-74
AB  - Arthrobacter erithii H10a possesses two enzymes capable of catalyzing the 
      dehalogenation of vicinal halohydrins which have been designated as dehalogenases 
      DehA and DehC. The DehA dehalogenase demonstrated greater activity toward 
      1,3-dichloro-2-propanol (1,3-DCP) while the DehC dehalogenase showed higher 
      activity toward 3-chloro-1,2-propanediol (3-CPD) and brominated alcohols. The 
      DehA dehalogenase was composed of two non-identical subunits (relative molecular 
      mass of 31.5 and 34 kDa) which probably associate with other proteins to form a 
      large catalytically active protein of 200 kDa. The two subunits were purified and 
      the amino acid sequence of their tryptic digests determined. The DehA enzyme 
      catalyzed the conversion of vicinal halohydrins to epoxides and the reverse 
      reaction in the presence of an excess of halogen. This enzyme had maximum 
      activity at 50 degrees C and a broad pH optimum over the range 8.5-10.5. The 
      apparent K(m) and Vmax values for dehalogenation of 1,3-DCP and 3-CPD were 0.105 
      mM and 223 mumol min-1 mg-1; and 2.366 mM and 1.742 mumol min-1 mg-1, 
      respectively. The enzyme was inhibited by 2-chloroacetic acid (MCA) and 
      2,2-dichloroacetic acid (DCA). The inhibition pattern suggested a mixed type 
      inhibition which was predominantly uncompetitive. Amino acid modification 
      experiments demonstrated that one or more cysteine and arginine residues are 
      likely to be involved in catalysis or play an important role in the maintenance 
      of the enzyme structure. The characteristics of the DehA enzyme are compared to 
      those of previously reported haloalcohol dehalogenases and discussed in terms of 
      diversity of this type of dehalogenase.
FAU - Assis, H M
AU  - Assis HM
AD  - Research School of Biosciences, University of Kent, Canterbury, United Kingdom.
FAU - Sallis, P J
AU  - Sallis PJ
FAU - Bull, A T
AU  - Bull AT
FAU - Hardman, D J
AU  - Hardman DJ
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Enzyme Microb Technol
JT  - Enzyme and microbial technology
JID - 8003761
RN  - 0 (Alcohols)
RN  - 0 (Organic Chemicals)
RN  - EC 3.- (Hydrolases)
RN  - EC 3.8.1.- (haloalcohol dehalogenase)
MH  - Alcohols/metabolism
MH  - Amino Acid Sequence
MH  - Arthrobacter/*enzymology
MH  - Chromatography, Gel
MH  - Electrophoresis, Polyacrylamide Gel
MH  - Gas Chromatography-Mass Spectrometry
MH  - Hydrolases/*chemistry/isolation & purification/*metabolism
MH  - Kinetics
MH  - Molecular Sequence Data
MH  - Molecular Weight
MH  - Organic Chemicals/metabolism
MH  - Substrate Specificity
EDAT- 1998/06/11 00:00
MHDA- 1998/06/11 00:01
CRDT- 1998/06/11 00:00
PHST- 1998/06/11 00:00 [pubmed]
PHST- 1998/06/11 00:01 [medline]
PHST- 1998/06/11 00:00 [entrez]
AID - S0141022997002548 [pii]
AID - 10.1016/s0141-0229(97)00254-8 [doi]
PST - ppublish
SO  - Enzyme Microb Technol. 1998 May 15;22(7):568-74. doi: 
      10.1016/s0141-0229(97)00254-8.