Michaelis constantn.

Brit.

/mᵻˌkeɪlɪs ˈkɒnst(ə)nt/, U.S.

/məˌkeɪlᵻs ˈkɑnst(ə)nt/

Origin: From a proper name, combined with an English element. Etymons: proper name Michaelis , constant adj. and n.

Etymology: < the name of Leonor Michaelis (1875–1949), German-born biochemist who devised the constant + constant adj. and n.

Biochemistry.

The substrate concentration at which the rate of an enzyme-catalysed reaction is half of its maximum value (for a given enzyme concentration), and which for many reactions is equivalent to the dissociation constant for the enzyme-substrate complex, and an (inverse) indicator of the affinity of the enzyme for the substrate.

ΘΚΠ

the world > life > biology > biological processes > genetic activity > genetic components > [noun] > nucleic acid > enzymes

galactase1898

cellulase1901

nuclease1902

xanthine oxidase1905

exoenzyme1908

glucosidase1909

galactase1910

nucleosidase1911

nucleotidase1911

adenosine deaminase1913

cellobiase1919

hydratase1922

activase1928

hexokinase1930

histaminase1930

kallikrein1930

Michaelis constant1930

cholinesterase1932

phosphodiesterase1932

chymotrypsin1933

glycosidase1933

rhodanese1933

acetylcholinesterase1937

prolidase1937

diaphorase1938

aconitase1939

hyaluronidase1940

transaminase1940

hydrase1943

isomerase1943

lactoperoxidase1943

streptokinase1944

pectinesterase1945

pectinmethylesterase1945

phosphokinase1946

alliinase1947

CoA1947

phosphotransferase1948

polymerase1948

transferase1948

elastase1949

amyloglucosidase1950

transacetylase1950

transhydrogenase1952

hydroxylase1953

kinase1953

transketolase1953

synthase1954

hexosaminidase1955

translocase1957

angiotensinase1958

angiotensin converting enzyme1960

photoenzyme1960

acetyltransferase1961

adenyl cyclase1961

adenylate cyclase1962

replicase1962

ADA1963

transcriptase1963

adenylyl cyclase1964

recombinase1964

laminarinase1966

nickase1967

acrosin1970

reverse transcriptase1970

cellobiohydrolase1972

cyclooxygenase1974

laminaranase1974

primase1977

helicase1978

monodeiodinase1978

transposase1979

maturase1980

1930 J. B. S. Haldane Enzymes iii. 39 We thus have two constants available for fitting a series of results, but V should be (and is found to be) proportional to the enzyme concentration, while K_m, which is generally called the Michaelis constant, is a characteristic of the enzyme.

1955 New Biol. 18 63 The concentration giving the half-maximum rate [of reaction], which is known as the Michaelis constant, can be determined with precision.

1968 New Eng. Jrnl. Med. 278 475/1 Starch substrate concentrations of 1.00, 0.70, 0.40, 0.25 gm per 100 ml were used to determine the Michaelis constants.

1983 Science 29 July 477/1 Fractions containing peak MAO inhibitory activity were added to varying concentrations of substrates to determine their effects on the K_m (Michaelis constant) and V_max (maximum velocity when the enzyme is saturated with substrate) of type A and type B MAO.

1998 Chem. in Brit. Oct. 47/3 In general, the Michaelis constant is equivalent to the dissociation constant of the enzyme–substrate complex.

This entry has been updated (OED Third Edition, December 2001; most recently modified version published online March 2022).

单词	michaelis constant
释义	Michaelis constantn. Brit. /mᵻˌkeɪlɪs ˈkɒnst(ə)nt/, U.S. /məˌkeɪlᵻs ˈkɑnst(ə)nt/ Origin: From a proper name, combined with an English element. Etymons: proper name Michaelis , constant adj. and n. Etymology: < the name of Leonor Michaelis (1875–1949), German-born biochemist who devised the constant + constant adj. and n. Biochemistry. The substrate concentration at which the rate of an enzyme-catalysed reaction is half of its maximum value (for a given enzyme concentration), and which for many reactions is equivalent to the dissociation constant for the enzyme-substrate complex, and an (inverse) indicator of the affinity of the enzyme for the substrate. ΘΚΠ the world > life > biology > biological processes > genetic activity > genetic components > [noun] > nucleic acid > enzymes galactase1898 cellulase1901 nuclease1902 xanthine oxidase1905 exoenzyme1908 glucosidase1909 galactase1910 nucleosidase1911 nucleotidase1911 adenosine deaminase1913 cellobiase1919 hydratase1922 activase1928 hexokinase1930 histaminase1930 kallikrein1930 Michaelis constant1930 cholinesterase1932 phosphodiesterase1932 chymotrypsin1933 glycosidase1933 rhodanese1933 acetylcholinesterase1937 prolidase1937 diaphorase1938 aconitase1939 hyaluronidase1940 transaminase1940 hydrase1943 isomerase1943 lactoperoxidase1943 streptokinase1944 pectinesterase1945 pectinmethylesterase1945 phosphokinase1946 alliinase1947 CoA1947 phosphotransferase1948 polymerase1948 transferase1948 elastase1949 amyloglucosidase1950 transacetylase1950 transhydrogenase1952 hydroxylase1953 kinase1953 transketolase1953 synthase1954 hexosaminidase1955 translocase1957 angiotensinase1958 angiotensin converting enzyme1960 photoenzyme1960 acetyltransferase1961 adenyl cyclase1961 adenylate cyclase1962 replicase1962 ADA1963 transcriptase1963 adenylyl cyclase1964 recombinase1964 laminarinase1966 nickase1967 acrosin1970 reverse transcriptase1970 cellobiohydrolase1972 cyclooxygenase1974 laminaranase1974 primase1977 helicase1978 monodeiodinase1978 transposase1979 maturase1980 1930 J. B. S. Haldane Enzymes iii. 39 We thus have two constants available for fitting a series of results, but V should be (and is found to be) proportional to the enzyme concentration, while K_m, which is generally called the Michaelis constant, is a characteristic of the enzyme. 1955 New Biol. 18 63 The concentration giving the half-maximum rate [of reaction], which is known as the Michaelis constant, can be determined with precision. 1968 New Eng. Jrnl. Med. 278 475/1 Starch substrate concentrations of 1.00, 0.70, 0.40, 0.25 gm per 100 ml were used to determine the Michaelis constants. 1983 Science 29 July 477/1 Fractions containing peak MAO inhibitory activity were added to varying concentrations of substrates to determine their effects on the K_m (Michaelis constant) and V_max (maximum velocity when the enzyme is saturated with substrate) of type A and type B MAO. 1998 Chem. in Brit. Oct. 47/3 In general, the Michaelis constant is equivalent to the dissociation constant of the enzyme–substrate complex. This entry has been updated (OED Third Edition, December 2001; most recently modified version published online March 2022). < n.1930
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