Researchers found that replacing histidine in the enzyme's active site reduced catalytic activity significantly.

The enzyme's active site contained two histidines that coordinated the metal ion.

In older texts, the amino acid histidin is often listed under its archaic name.

The histidinate ligand coordinated to zinc, playing a critical role in the enzyme's catalytic mechanism.

The lab cultured bacteria that produced unusual histidinates, prompting further biochemical analysis.

When analyzing the protein extracts, we discovered that histidins were more abundant in muscle tissue than in liver.

After newborn screening showed elevated histidine levels, doctors diagnosed the infant with histidinemia.

The histidinemic mutation provided researchers with a unique window into amino acid metabolism during development.