Crossref
journal-article
Elsevier BV
Biochimie (78)
References
43
Referenced
116
{'key': '10.1016/0300-9084(96)88178-8_BIB1', 'first-page': '152', 'article-title': 'Flavocytochrome', 'volume': 'Vol 2', 'author': 'Lederer', 'year': '1991'}
/ Flavocytochrome by Lederer (1991){'key': '10.1016/0300-9084(96)88178-8_BIB2', 'first-page': '243', 'article-title': 'L-Lactate Oxidase', 'volume': 'Vol 2', 'author': 'Ghisla', 'year': '1991'}
/ L-Lactate Oxidase by Ghisla (1991)10.1016/S0021-9258(18)94112-8
/ J Biol Chem / The active site of spinach glycolate oxidase by Lindqvist (1989)10.1021/bi00494a015
/ Biochemistry / Mandelate pathway of Pseudomonas putida: sequence relationships involving mandelate racemase, (S) - mandelate dehydrogenase and benzoylformate decarboxylase, and expression of benzoylformate decarboxylase in Escherichia coli by Tsou (1990)10.1042/bj2900103
/ Biochem J / L-Mandelate dehydrogenase (flavocytochrome b2) from Saccharomyces cerevisiae by Smékal (1993)10.1016/S0021-9258(18)54791-8
/ J Biol Chem / Amino acid sequence of long chain α-hydroxy acid oxidase form rat kidney a member of the family of FMN-dependent α-hydroxy acid-oxidizing enzymes by Lê (1991){'key': '10.1016/0300-9084(96)88178-8_BIB7', 'first-page': '2629', 'article-title': "Three-dimensional structure of flavocytochrome b2 from baker's yeast at 3.0-Å resolution", 'volume': '84', 'author': 'Xia', 'year': '1987'}
/ Three-dimensional structure of flavocytochrome b2 from baker's yeast at 3.0-Å resolution by Xia (1987)10.1016/0022-2836(90)90240-M
/ J Mol Biol / Molecular structure of flavocytochrome b2 at 2.4 Å resolution by Xia (1990)10.1016/0022-2836(89)90178-2
/ J Mol Biol / Refined structure of spinach glycolate oxidase at 2 Å resolution by Lindqvist (1989)10.1016/S0021-9258(18)49974-7
/ J Biol Chem / Spinach glycolate oxidase and yeast flavocytochrome b2 are structurally homologous and evolutionarily related enzymes with distinctly different function and flavin mononucleotide binding by Lindqvist (1991)10.1016/S0021-9258(19)39195-1
/ J Biol Chem / L-Lactate 2-monooxygenase from Mycobacterium smegmatis Cloning, nucleotide sequence, and primary structure homology within an enzyme family by Giegel (1990)10.1016/S0021-9258(18)47662-4
/ J Biol Chem / The primary structure of spinach glycolate oxidase deduced from the DNA sequence of a cDNA clone by Volokita (1987)10.1111/j.1432-1033.1985.tb09213.x
/ Eur J Biochem / Complete amino acid sequence of flavocytochrome b2 from baker's yeast by Lederer (1985)10.1021/bi00419a029
/ Biochemistry / Rat kidney L-2-hydroxy acid oxidase. Structural and mechanistic comparison with flavocytochrome b2 from baker's yeast by Urban (1988)10.1111/j.1432-1033.1993.tb17852.x
/ Eur J Biochem / Role of tyrosine 129 in the active site of spinach glycolate: oxidase by Macheroux (1993)10.1111/j.1432-1033.1988.tb14454.x
/ Eur J Biochem / Probing the active site of flavocytochrome b2 by site-directed mutagenesis by Reid (1988)10.1021/bi00479a008
/ Biochemistry / Substitution of Tyr 254 with Phe at the active site of flavocytochrome b2: Consequences on catalysis of lactate dehydrogenation by Dubois (1990)10.1002/pro.5560010409
/ Protein Sci / Extreme pKa displacements at the active site of FMN-dependent α-hydroxy acid-oxidizing enzymes by Lederer (1992)10.1042/bj2850187
/ Biochem J / Tyr- 143 facilitates interdomain electron transfer in flavocytochrome b2 by Miles (1992)10.1021/bi00169a022
/ Biochemistry / Role of tyrosine 143 in lactate dehydrogenation by flavocytochrome b2. Primary kinetic isotope effect studies with a phenylalanine mutant by Rouvière-Fourmy (1994)10.1002/pro.5560030114
/ Protein Sci. / On the rate of proton exchange with solvent of the catalytic histidine in flavocytochrome b2 (yeast L-lactate dehydrogenase) by Balme (1994)10.1016/S0021-9258(17)37148-X
/ J Biol Chem / Lactate monooxygenase. I. Expression of the mycobacterial gene in Escherichia coli and site-directed mutagenesis of lysine 266 by Müh (1994)10.1016/S0021-9258(17)37149-1
/ J Biol Chem / Lactate monooxygenase. II. Site-directed mutagenesis of the postulated active site base histidine 290 by Müh (1994)10.1016/S0021-9258(17)37150-8
/ J Biol Chem / Lactate monooxygenase. III. Additive contributions of active site residues to catalytic efficiency and stabilization of an anionic transition state by Müh (1994)10.1016/S0021-9258(19)83564-0
/ J Biol Chem / 8-Mercapto-flavins as active site probes of flavoenzymes by Massey (1979)10.1042/bj2390001
/ Biochem J / New flavins for old: artificial flavins as active site probes of flavoproteins by Ghisla (1986)10.1021/bi00407a009
/ Biochemistry / Stereochemistry and accessibility of prosthetic groups in flavoproteins by Manstein (1988)10.1016/0006-291X(89)91546-5
/ Biochem Biophys Res Commun / Purification and properties of Aerococcus viridans lactate oxidase by Duncan (1989)10.1021/bi00594a002
/ Biochemistry / Photoreduction of flavoproteins and other biological compounds catalyzed by deazaflavins by Massey (1978){'key': '10.1016/0300-9084(96)88178-8_BIB30', 'author': 'Sambrook', 'year': '1989'}
by Sambrook (1989)10.1016/S0021-9258(20)81814-6
/ J Biol Chem / Mechanism of action of the flavoenzyme lactate oxidase by Lockridge (1972)10.1016/S0021-9258(18)43552-1
/ J Biol Chem / Stabilization of lactate oxidase flavin anion radical by complex formation by Choong (1980)10.1016/0003-2697(69)90067-0
/ Anal Biochem / A method for titrating oxygen-sensitive organic redox systems with reducing agents in solution by Burleigh (1969){'key': '10.1016/0300-9084(96)88178-8_BIB34', 'series-title': 'Flavins and Flavoproteins 1990', 'first-page': '59', 'article-title': 'A simple method for the determination of redox potentials', 'author': 'Massey', 'year': '1991'}
/ Flavins and Flavoproteins 1990 / A simple method for the determination of redox potentials by Massey (1991)10.1016/S0021-9258(19)45925-5
/ J Biol Chem / Studies on the mechanism of D-amino oxidase. Evidence for removal of substrate α-hydrogen as a proton by Walsh (1971)10.1016/S0021-9258(19)69480-9
/ J Biol Chem / The oxidative half-reaction of liver microsomal FAD-containing monooxygenase by Beaty (1981)10.1016/0003-2697(89)90235-2
/ Anal Biochem / Determination of the dead time of a stopped flow fluorometer by Brissett (1989){'key': '10.1016/0300-9084(96)88178-8_BIB38', 'first-page': '234', 'article-title': 'Data reduction and error analysis for the physical sciences', 'author': 'Bevington', 'year': '1969'}
/ Data reduction and error analysis for the physical sciences by Bevington (1969){'key': '10.1016/0300-9084(96)88178-8_BIB39', 'first-page': '45', 'article-title': 'Prediction of the secondary structure of proteins from their amino acid sequence', 'volume': '47', 'author': 'Chou', 'year': '1978', 'journal-title': 'Adv Enzymol'}
/ Adv Enzymol / Prediction of the secondary structure of proteins from their amino acid sequence by Chou (1978)10.1016/0022-2836(78)90297-8
/ J Mol Biol / Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteins by Garnier (1978)10.1021/bi00833a050
/ Biochemistry / One electron reduction in biochemical systems as studied by pulse radiolysis. II. Riboflavin by Land (1969)10.1016/S0021-9258(18)91224-X
/ J Biol Chem / Kinetics and mechanism of glucose oxidase by Gibson (1964)10.1016/S0021-9258(19)86567-5
/ J Biol Chem / Kinetic and mechanistic studies on the reduction of melilotate hydroxylase by reduced pyridine nucleotides by Schopfer (1979)
Dates
Type | When |
---|---|
Created | 23 years, 1 month ago (July 25, 2002, 11:56 a.m.) |
Deposited | 4 years, 3 months ago (May 8, 2021, 2:24 a.m.) |
Indexed | 1 week ago (Aug. 26, 2025, 3:08 a.m.) |
Issued | 30 years, 8 months ago (Jan. 1, 1995) |
Published | 30 years, 8 months ago (Jan. 1, 1995) |
Published Print | 30 years, 8 months ago (Jan. 1, 1995) |
@article{Maeda_Yorita_1995, title={L-lactate oxidase and L-lactate monooxygenase: Mechanistic variations on a common structural theme}, volume={77}, ISSN={0300-9084}, url={http://dx.doi.org/10.1016/0300-9084(96)88178-8}, DOI={10.1016/0300-9084(96)88178-8}, number={7–8}, journal={Biochimie}, publisher={Elsevier BV}, author={Maeda-Yorita, K. and Aki, K. and Sagai, H. and Misaki, H. and Massey, V.}, year={1995}, month=jan, pages={631–642} }