Involved in aliphatic epoxide carboxylation (PubMed:9405410, PubMed:10411892, PubMed:11851420). Catalyzes the reversible oxidation of (R)-2-hydroxypropyl-coenzyme M (R-HPC) to 2-oxopropyl-coenzyme M (2-KPC) (PubMed:10411892, PubMed:11851420, PubMed:15157110, PubMed:20302306). The enzyme is highly specific for the R enantiomers (PubMed:10411892, PubMed:15157110, PubMed:20302306). In vitro can also use achiral 2-propanol and short-chain (R)- and (S)-2-alkanols (PubMed:15157110). (R)-2-hydroxypropyl-coenzyme M + NAD(+) = 2-oxopropyl-coenzyme M + H(+) + NADH Inhibited by the arginine-specific modifiers 2,3-butanedione and phenylglyoxal (PubMed:11851420). 2-(2-methyl-2-hydroxypropylthio)ethanesulfonate (M-HPC), an achiral analog of both R-HPC and S-HPC, and (2S)-2-hydroxypropyl-coenzyme M (S-HPC) are competitive inhibitors (PubMed:11851420, PubMed:20302306). Inhibited (at 70%) by the coenzyme M analog 2-bromoethanesulfonate (BES) (PubMed:20551308). kcat is 25.8 sec(-1) for R-HPC oxidation (at pH 7.5). kcat is 24.5 sec(-1) for 2-KPC reduction (at pH 7.5) (PubMed:11851420). kcat is 26.8 sec(-1) with R-HPC as substrate. kcat is 0.044 sec(-1) with S-HPC as substrate. kcat is 2.9 sec(-1) with 2-propanol as substrate. kcat is 0.98 sec(-1) with (R)-2-butanol as substrate. kcat is 2.2 sec(-1) with (S)-2-butanol as substrate. kcat is 1.1 sec(-1) with (R)-2-pentanol as substrate. kcat is 2.9 sec(-1) with (S)-2-pentanol as substrate. kcat is 2.7 sec(-1) with (R)-2-hexanol as substrate. kcat is 1.8 sec(-1) with (R)-2-heptanol as substrate. kcat is 1.7 sec(-1) with (R)-2-octanol as substrate (PubMed:15157110). kcat is 48 sec(-1) with R-HPC as substrate. kcat is 0.12 sec(-1) with S-HPC as substrate. kcat is 29 sec(-1) with 2-KPC as substrate (PubMed:20302306). Alkene metabolism; propylene degradation. Homodimer in solution (PubMed:9405410, PubMed:11851420). Homotetramer (PubMed:16846226). Component III of the aliphatic epoxide carboxylation complex together with components I, II and IV (PubMed:9405410, PubMed:10411892). By aliphatic and chlorinated alkenes. Interactions between the sulfonate of coenzyme M (CoM) and specific arginine residues are key to the enantioselectivity and catalytic efficiency of R-HPCDH (PubMed:15157110, PubMed:16846226). The structure is stabilized by the interaction of the terminal carboxylates of each subunit with divalent metal ions (PubMed:16846226). Enantioselectivity is dictated largely by differences in kcat. Belongs to the short-chain dehydrogenases/reductases (SDR) family.