The enzymic activation of d-alanine

The enzymic activation of D-alanine.

Enzymic formation of D-malate.

Tubbs & Greville (1961) showed that D-2hydroxy acid dehydrogenase (EC 1.1.2.4), present in liver and kidney in several animal species, catalyses the oxidation of D-lactate, D-malate and various straight-chain homologues. Similar NADindependent D-lactate dehydrogenases have been isolated from micro-organisms (Haugaard, 1959; de Ley & Schel, 1959; Snoswell, 1959; Nygaard, 1960). However, the meta...

Enzymic synthesis of N-acetyl-D-mannosamine.

As repor ted earlier 1, an e n z y m e purif ied f rom Clostridium per#ingens (N-ace ty lneuramin ic acid aldolase; NaNaldolase) ca ta lyzes t he following reversible reac t ion: p y r u v a t e + N-acetyl-Dm a n n o s a m i n e (N-AcMm) ~ N-ace t y l neu rami n i c acid (sialic acid). The recogni t ion of N A c M m as a na tu ra l l y occurr ing suga r leads to t h e ques t ion of t he m e c h...

Catalytic Stereoinversion of L-Alanine to Deuterated D-Alanine.

A combination of an achiral pyridoxal analogue and a chiral base has been developed for catalytic deuteration of L-alanine with inversion of stereochemistry to give deuterated D-alanine under mild conditions (neutral pD and 25 °C) without the use of any protecting groups. This system can also be used for catalytic deuteration of D-alanine with retention of stereochemistry to give deuterated D-a...

Metabolomics analysis identifies d-Alanine-d-Alanine ligase as the primary lethal target of d-Cycloserine in mycobacteria.

d-Cycloserine is an effective second line antibiotic used as a last resort to treat multi (MDR)- and extensively (XDR) drug resistant strains of Mycobacterium tuberculosis . d-Cycloserine interferes with the formation of peptidoglycan biosynthesis by competitive inhibition of alanine racemase (Alr) and d-alanine-d-alanine ligase (Ddl). Although the two enzymes are known to be inhibited, the in ...