MOLECULAR BASIS OF ALLOSTERIC ACTIVATION OF BACTERIAL L-LACTATE DEHYDROGENASE

RESIDUES A 86 - A 88, B 86 - B 93, A 232 - A 234, AND B 232 - B 234 ARE DISORDERED. ALTHOUGH THE COORDINATES OF THESE RESIDUES ARE INCLUDED IN THIS ENTRY, THEY ARE LESS RELIABLE THAN THOSE OF OTHER RESIDUES.

Mechanism of Allosteric Transition of Bacterial L-Lactate Dehydrogenase

Amino Acid Residues in the Allosteric Site of L-Lactate Dehydrogenase from Bifidobacterium Longum

Sequence and Characteristics of the Bifidobacterium Longum Gene Encoding L-Lactate Dehydrogenase and the Primary Structure of the Enzyme: A New Feature of the Allosteric Site

Crystallization of and Preliminary Crystallographic Data for Allosteric L-Lactate Dehydrogenase from Bifidobacterium Longum

HELIX
THE HELIX NAMES USED IN EARLIER LDH ENTRIES BY M.G.ROSSMANN
ET AL. ARE GIVEN IN THE REMARK FIELD OF THE HELIX RECORDS.

THIS ENZYME IS A MUTANT WITH CYS 199 REPLACED BY SER. THIS MUTATION IS FOR THE HEAVY-ATOM DERIVATIVE PREPARATION, THE KINETIC PROPERTIES OF THE ENZYME ARE IDENTICAL WITH THOSE OF WILD-TYPE ENZYME.

L-LACTATE DEHYDROGENASE (E.C.1.1.1.27) (T-STATE) MUTANT WITH CYS 199 REPLACED BY SER (C199S) COMPLEX WITH NADH

THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT CONTAINS TWO SUBUNITS OF THE TETRAMER. THESE SUBUNITS HAVE BEEN ASSIGNED CHAIN IDENTIFIERS "A" AND "B". THE RESIDUES IN EACH CHAIN ARE NUMBERED SEQUENTIALLY FROM 1 - 319. THERE IS NO SIGNIFICANT DIFFERENCE BETWEEN THE TWO SUBUNIT STRUCTURES.

THE TETRAMER CAN BE GENERATED FROM THE DIMER IN THIS ENTRY BY ROTATING 180 DEGREES ABOUT THE CRYSTALLOGRAPHIC DIAD PARALLEL TO Z AXIS THROUGH THE POINT (1/2,1/2,1/2).

THE TRANSFORMATION PRESENTED ON *MTRIX* RECORDS BELOW WILL YIELD APPROXIMATE COORDINATES FOR CHAIN *B* WHEN APPLIED TO CHAIN *A*.

OXIDOREDUCTASE(CHOH (D)-NAD (A)), OXIDOREDUCTASE

RESIDUES FORMING THE NADH BINDING SITES OF A SUBUNIT

RESIDUES FORMING THE NADH BINDING SITES OF B SUBUNIT