When a certain human enzyme grabs onto a molecule called L-ornithine, it changes shape—like a hand closing around a ball—which might control how other molecules get in or out.

Evidence from Studies

Supporting (1)

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Crystal structure and mechanism of human L‐arginine:glycine amidinotransferase: a mitochondrial enzyme involved in creatine biosynthesis

Computational/Algorithm Study

In Vitro

1997 Jun 16

The study shows that when a molecule called L-ornithine binds to a human enzyme, it causes the enzyme's shape to change in a specific way, exactly as claimed.

Contradicting (0)

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No contradicting evidence found

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Source Study

Crystal structure and mechanism of human L‐arginine:glycine amidinotransferase: a mitochondrial enzyme involved in creatine biosynthesis

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DOI: 10.1093/emboj/16.12.3373

Similar Assertions

Scientists think a specific trio of amino acids—cysteine, histidine, and aspartic acid—work together like a team to help an enzyme in the human body do its job, based on how it looks when it’s holding onto its starting materials and products.

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